A family of large adaptin protein subunits of approximately 100 kDa in size. They have been primarily found as components of ADAPTOR PROTEIN COMPLEX 2.
An adaptor protein complex found primarily on perinuclear compartments.
A clathrin adaptor protein complex primarily involved in clathrin-related transport at the TRANS-GOLGI NETWORK.
An adaptor protein complex primarily involved in the formation of clathrin-related endocytotic vesicles (ENDOSOMES) at the CELL MEMBRANE.
An adaptor protein complex involved in transport of molecules between the TRANS-GOLGI NETWORK and the endosomal-lysosomal system.
The subunits that make up the large, medium and small chains of adaptor proteins.
A family of large adaptin protein subunits of approximately 130-kDa in size. They have been primarily found as components of ADAPTOR PROTEIN COMPLEX 3.
A family of medium adaptin protein subunits of approximately 45 KDa in size. They have been primarily found as components of ADAPTOR PROTEIN COMPLEX 3 and ADAPTOR PROTEIN COMPLEX 4.
A class of proteins involved in the transport of molecules via TRANSPORT VESICLES. They perform functions such as binding to the cell membrane, capturing cargo molecules and promoting the assembly of CLATHRIN. The majority of adaptor proteins exist as multi-subunit complexes, however monomeric varieties have also been found.
A family of large adaptin protein subunits of approximately 90 KDa in size. They have been primarily found as components of ADAPTOR PROTEIN COMPLEX 1.
A family of large adaptin protein complex subunits of approximately 90-130 kDa in size.
A broad category of carrier proteins that play a role in SIGNAL TRANSDUCTION. They generally contain several modular domains, each of which having its own binding activity, and act by forming complexes with other intracellular-signaling molecules. Signal-transducing adaptor proteins lack enzyme activity, however their activity can be modulated by other signal-transducing enzymes
The main structural coat protein of COATED VESICLES which play a key role in the intracellular transport between membranous organelles. Each molecule of clathrin consists of three light chains (CLATHRIN LIGHT CHAINS) and three heavy chains (CLATHRIN HEAVY CHAINS) that form a structure called a triskelion. Clathrin also interacts with cytoskeletal proteins.
The fundamental dispositions and traits of humans. (Merriam-Webster's Collegiate Dictionary, 10th ed)
A subclass of clathrin assembly proteins that occur as monomers.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Single chains of amino acids that are the units of multimeric PROTEINS. Multimeric proteins can be composed of identical or non-identical subunits. One or more monomeric subunits may compose a protomer which itself is a subunit structure of a larger assembly.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A signal transducing adaptor protein that links extracellular signals to the MAP KINASE SIGNALING SYSTEM. Grb2 associates with activated EPIDERMAL GROWTH FACTOR RECEPTOR and PLATELET-DERIVED GROWTH FACTOR RECEPTORS via its SH2 DOMAIN. It also binds to and translocates the SON OF SEVENLESS PROTEINS through its SH3 DOMAINS to activate PROTO-ONCOGENE PROTEIN P21(RAS).
A family of signaling adaptor proteins that contain SRC HOMOLOGY DOMAINS. Many members of this family are involved in transmitting signals from CELL SURFACE RECEPTORS to MITOGEN-ACTIVATED PROTEIN KINASES.
A family of small adaptin protein complex subunits of approximately 19 KDa in size.
Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
Vesicles formed when cell-membrane coated pits (COATED PITS, CELL-MEMBRANE) invaginate and pinch off. The outer surface of these vesicles are covered with a lattice-like network of coat proteins, such as CLATHRIN, coat protein complex proteins, or CAVEOLINS.
The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.
A network of membrane compartments, located at the cytoplasmic side of the GOLGI APPARATUS, where proteins and lipids are sorted for transport to various locations in the cell or cell membrane.
Vesicles formed when cell-membrane coated pits (COATED PITS, CELL-MEMBRANE) invaginate and pinch off. The outer surface of these vesicles is covered with a lattice-like network of the protein CLATHRIN. Shortly after formation, however, the clathrin coat is removed and the vesicles are referred to as ENDOSOMES.
Cytoplasmic vesicles formed when COATED VESICLES shed their CLATHRIN coat. Endosomes internalize macromolecules bound by receptors on the cell surface.
Transport proteins that carry specific substances in the blood or across cell membranes.
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
Established cell cultures that have the potential to propagate indefinitely.
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
Phosphoproteins are proteins that have been post-translationally modified with the addition of a phosphate group, usually on serine, threonine or tyrosine residues, which can play a role in their regulation, function, interaction with other molecules, and localization within the cell.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
Vesicles that are involved in shuttling cargo from the interior of the cell to the cell surface, from the cell surface to the interior, across the cell or around the cell to various locations.
The GTPase-containing subunits of heterotrimeric GTP-binding proteins. When dissociated from the heterotrimeric complex these subunits interact with a variety of second messenger systems. Hydrolysis of GTP by the inherent GTPase activity of the subunit causes it to revert to its inactive (heterotrimeric) form. The GTP-Binding protein alpha subunits are grouped into families according to the type of action they have on second messenger systems.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
Regulatory proteins that act as molecular switches. They control a wide range of biological processes including: receptor signaling, intracellular signal transduction pathways, and protein synthesis. Their activity is regulated by factors that control their ability to bind to and hydrolyze GTP to GDP. EC 3.6.1.-.
Specialized regions of the cell membrane composed of pits coated with a bristle covering made of the protein CLATHRIN. These pits are the entry route for macromolecules bound by cell surface receptors. The pits are then internalized into the cytoplasm to form the COATED VESICLES.
The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.
Macromolecular complexes formed from the association of defined protein subunits.
A binding partner for several RECEPTOR PROTEIN-TYROSINE KINASES, including INSULIN RECEPTOR and INSULIN-LIKE GROWTH FACTOR RECEPTOR. It contains a C-terminal SH2 DOMAIN and mediates various SIGNAL TRANSDUCTION pathways.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
Products of the retroviral NEF GENE. They play a role as accessory proteins that influence the rate of viral infectivity and the destruction of the host immune system. nef gene products were originally found as factors that trans-suppress viral replication and function as negative regulators of transcription. nef stands for negative factor.

AP-4, a novel protein complex related to clathrin adaptors. (1/230)

Here we report the identification and characterization of AP-4, a novel protein complex related to the heterotetrameric AP-1, AP-2, and AP-3 adaptors that mediate protein sorting in the endocytic and late secretory pathways. The key to the identification of this complex was the cloning and sequencing of two widely expressed, mammalian cDNAs encoding new homologs of the adaptor beta and sigma subunits named beta4 and sigma4, respectively. An antibody to beta4 recognized in human cells an approximately 83-kDa polypeptide that exists in both soluble and membrane-associated forms. Gel filtration, sedimentation velocity, and immunoprecipitation experiments revealed that beta4 is a component of a multisubunit complex (AP-4) that also contains the sigma4 polypeptide and two additional adaptor subunit homologs named mu4 (mu-ARP2) and epsilon. Immunofluorescence analyses showed that AP-4 is associated with the trans-Golgi network or an adjacent structure and that this association is sensitive to the drug brefeldin A. We propose that, like the related AP-1, AP-2, and AP-3 complexes, AP-4 plays a role in signal-mediated trafficking of integral membrane proteins in mammalian cells.  (+info)

High-affinity binding of the AP-1 adaptor complex to trans-golgi network membranes devoid of mannose 6-phosphate receptors. (2/230)

The GTP-binding protein ADP-ribosylation factor (ARF) initiates clathrin-coat assembly at the trans-Goli network (TGN) by generating high-affinity membrane-binding sites for the AP-1 adaptor complex. Both transmembrane proteins, which are sorted into the assembling coated bud, and novel docking proteins have been suggested to be partners with GTP-bound ARF in generating the AP-1-docking sites. The best characterized, and probably the major transmembrane molecules sorted into the clathrin-coated vesicles that form on the TGN, are the mannose 6-phosphate receptors (MPRs). Here, we have examined the role of the MPRs in the AP-1 recruitment process by comparing fibroblasts derived from embryos of either normal or MPR-negative animals. Despite major alterations to the lysosome compartment in the MPR-deficient cells, the steady-state distribution of AP-1 at the TGN is comparable to that of normal cells. Golgi-enriched membranes prepared from the receptor-negative cells also display an apparently normal capacity to recruit AP-1 in vitro in the presence of ARF and either GTP or GTPgammaS. The AP-1 adaptor is recruited specifically onto the TGN and not onto the numerous abnormal membrane elements that accumulate within the MPR-negative fibroblasts. AP-1 bound to TGN membranes from either normal or MPR-negative fibroblasts is fully resistant to chemical extraction with 1 M Tris-HCl, pH 7, indicating that the adaptor binds to both membrane types with high affinity. The only difference we do note between the Golgi prepared from the MPR-deficient cells and the normal cells is that AP-1 recruited onto the receptor-lacking membranes in the presence of ARF1.GTP is consistently more resistant to extraction with Tris. Because sensitivity to Tris extraction correlates well with nucleotide hydrolysis, this finding might suggest a possible link between MPR sorting and ARF GAP regulation. We conclude that the MPRs are not essential determinants in the initial steps of AP-1 binding to the TGN but, instead, they may play a regulatory role in clathrin-coated vesicle formation by affecting ARF.GTP hydrolysis.  (+info)

Cluster of differentiation antigen 4 (CD4) endocytosis and adaptor complex binding require activation of the CD4 endocytosis signal by serine phosphorylation. (3/230)

Cluster of differentiation antigen 4 (CD4), the T lymphocyte antigen receptor component and human immunodeficiency virus coreceptor, is down-modulated when cells are activated by antigen or phorbol esters. During down-modulation CD4 dissociates from p56(lck), undergoes endocytosis through clathrin-coated pits, and is then sorted in early endosomes to late endocytic organelles where it is degraded. Previous studies have suggested that phosphorylation and a dileucine sequence are required for down-modulation. Using transfected HeLa cells, in which CD4 endocytosis can be studied in the absence of p56(lck), we show that the dileucine sequence in the cytoplasmic domain is essential for clathrin-mediated CD4 endocytosis. However, this sequence is only functional as an endocytosis signal when neighboring serine residues are phosphorylated. Phosphoserine is required for rapid endocytosis because CD4 molecules in which the cytoplasmic domain serine residues are substituted with glutamic acid residues are not internalized efficiently. Using surface plasmon resonance, we show that CD4 peptides containing the dileucine sequence bind weakly to clathrin adaptor protein complexes 2 and 1. The affinity of this interaction is increased 350- to 700-fold when the peptides also contain phosphoserine residues.  (+info)

The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis. (4/230)

betaarrestins mediate the desensitization of the beta2-adrenergic receptor (beta2AR) and many other G protein-coupled receptors (GPCRs). Additionally, betaarrestins initiate the endocytosis of these receptors via clathrin coated-pits and interact directly with clathrin. Consequently, it has been proposed that betaarrestins serve as clathrin adaptors for the GPCR family by linking these receptors to clathrin lattices. AP-2, the heterotetrameric clathrin adaptor protein, has been demonstrated to mediate the internalization of many types of plasma membrane proteins other than GPCRs. AP-2 interacts with the clathrin heavy chain and cytoplasmic domains of receptors such as those for epidermal growth factor and transferrin. In the present study we demonstrate the formation of an agonist-induced multimeric complex containing a GPCR, betaarrestin 2, and the beta2-adaptin subunit of AP-2. beta2-Adaptin binds betaarrestin 2 in a yeast two-hybrid assay and coimmunoprecipitates with betaarrestins and beta2AR in an agonist-dependent manner in HEK-293 cells. Moreover, beta2-adaptin translocates from the cytosol to the plasma membrane in response to the beta2AR agonist isoproterenol and colocalizes with beta2AR in clathrin-coated pits. Finally, expression of betaarrestin 2 minigene constructs containing the beta2-adaptin interacting region inhibits beta2AR endocytosis. These findings point to a role for AP-2 in GPCR endocytosis, and they suggest that AP-2 functions as a clathrin adaptor for the endocytosis of diverse classes of membrane receptors.  (+info)

Inhibition of clathrin-coated pit assembly by an Eps15 mutant. (5/230)

Recent data have shown that Eps15, a newly identified component of clathrin-coated pits constitutively associated with the AP-2 complex, is required for receptor-mediated endocytosis. However, its precise function remains unknown. Interestingly, Eps15 contains three EH (Eps15-Homology) domains also found in proteins required for the internalization step of endocytosis in yeast. Results presented here show that EH domains are required for correct coated pit targeting of Eps15. Furthermore, when cells expressed an Eps15 mutant lacking EH domains, the plasma membrane punctate distribution of both AP-2 and clathrin was lost, implying the absence of coated pits. This was further confirmed by the fact that dynamin, a GTPase found in coated pits, was homogeneously redistributed on the plasma membrane and that endocytosis of transferrin, a specific marker of clathrin-dependent endocytosis, was strongly inhibited. Altogether, these results strongly suggest a role for Eps15 in coated pit assembly and more precisely a role for Eps15 in the docking of AP-2 onto the plasma membrane. This hypothesis is supported by the fact that a GFP fusion protein encoding the ear domain of (alpha)-adaptin, the AP-2 binding site for Eps15, was efficiently targeted to plasma membrane coated pits.  (+info)

ADP-ribosylation factor 1 dependent clathrin-coat assembly on synthetic liposomes. (6/230)

The assembly of clathrin-coated vesicles on Golgi membranes is initiated by the GTP-binding protein ADP ribosylation factor (ARF), which generates high-affinity membrane-binding sites for the heterotetrameric AP-1 adaptor complex. Once bound, the AP-1 recruits clathrin triskelia, which polymerize to form the coat. We have found that ARF.GTP also recruits AP-1 and clathrin onto protein-free liposomes. The efficiency of this process is modulated by the composition of the liposomes, with phosphatidylserine being the most stimulatory phospholipid. There is also a requirement for cytosolic factor(s) other than ARF. Thin-section electron microscopy shows the presence of clathrin-coated buds and vesicles that resemble those formed in vivo. These results indicate that AP-1-containing clathrin-coated vesicles can form in the absence of integral membrane proteins. Thus, ARF.GTP, appropriate lipids, and cytosolic factor(s) are the minimal components necessary for AP-1 clathrin-coat assembly.  (+info)

Inhibition of the receptor-binding function of clathrin adaptor protein AP-2 by dominant-negative mutant mu2 subunit and its effects on endocytosis. (7/230)

Although interactions between the mu2 subunit of the clathrin adaptor protein complex AP-2 and tyrosine-based internalization motifs have been implicated in the selective recruitment of cargo molecules into coated pits, the functional significance of this interaction for endocytosis of many types of membrane proteins remains unclear. To analyze the function of mu2-receptor interactions, we constructed an epitope-tagged mu2 that incorporates into AP-2 and is targeted to coated pits. Mutational analysis revealed that Asp176 and Trp421 of mu2 are involved in the interaction with internalization motifs of TGN38 and epidermal growth factor (EGF) receptor. Inducible overexpression of mutant mu2, in which these two residues were changed to alanines, resulted in metabolic replacement of endogenous mu2 in AP-2 complexes and complete abrogation of AP-2 interaction with the tyrosine-based internalization motifs. As a consequence, endocytosis of the transferrin receptor was severely impaired. In contrast, internalization of the EGF receptor was not affected. These results demonstrate the potential usefulness of the dominant-interfering approach for functional analysis of the adaptor protein family, and indicate that clathrin-mediated endocytosis may proceed in both a mu2-dependent and -independent manner.  (+info)

Splice variants of intersectin are components of the endocytic machinery in neurons and nonneuronal cells. (8/230)

We recently identified and cloned intersectin, a protein containing two Eps15 homology (EH) domains and five Src homology 3 (SH3) domains. Using a newly developed intersectin antibody, we demonstrate that endogenous COS-7 cell intersectin localizes to clathrin-coated pits, and transfection studies suggest that the EH domains may direct this localization. Through alternative splicing in a stop codon, a long form of intersectin is generated with a C-terminal extension containing Dbl homology (DH), pleckstrin homology (PH), and C2 domains. Western blots reveal that the long form of intersectin is expressed specifically in neurons, whereas the short isoform is expressed at lower levels in glia and other nonneuronal cells. Immunofluorescence analysis of cultured hippocampal neurons reveals that intersectin is found at the plasma membrane where it is co-localized with clathrin. Ibp2, a protein identified based on its interactions with the EH domains of intersectin, binds to clathrin through the N terminus of the heavy chain, suggesting a mechanism for the localization of intersectin at clathrin-coated pits. Ibp2 also binds to the clathrin adaptor AP2, and antibodies against intersectin co-immunoprecipitate clathrin, AP2, and dynamin from brain extracts. These data suggest that the long and short forms of intersectin are components of the endocytic machinery in neurons and nonneuronal cells.  (+info)

Adaptor Protein Complex (AP) alpha subunits are a group of proteins that play a crucial role in intracellular trafficking, specifically in the formation and transport of vesicles within cells. There are four different AP complexes (AP-1, AP-2, AP-3, and AP-4), each with its own unique set of subunits, including an alpha subunit.

The AP-1 complex, for example, is involved in the transport of proteins between the Golgi apparatus and endosomes. Its alpha subunit, AP1A1 or AP1A2, helps to recognize specific sorting signals on protein cargo and facilitates the assembly of clathrin coats around vesicles.

Similarly, the AP-2 complex is involved in clathrin-mediated endocytosis at the plasma membrane, and its alpha subunit, AP2A1 or AP2A2, helps to recruit clathrin and other accessory proteins to form coated pits.

Mutations in genes encoding for AP complex subunits have been linked to various human diseases, including neurological disorders and cancer.

Adaptor Protein Complex 3 (APC3), also known as AP-3, is a type of adaptor protein complex that plays a crucial role in the sorting and trafficking of proteins within cells. It is composed of four subunits: delta, beta3A, mu3, and sigma3A. APC3 is primarily involved in the transport of proteins from the early endosomes to the lysosomes or to the plasma membrane. It also plays a role in the biogenesis of lysosome-related organelles such as melanosomes and platelet-dense granules. Mutations in the genes encoding for APC3 subunits have been associated with several genetic disorders, including Hermansky-Pudlak syndrome and Chediak-Higashi syndrome.

Adaptor Protein Complex 1 (AP-1) is a group of proteins that function as a complex to play a crucial role in the intracellular transport of various molecules, particularly in the formation of vesicles that transport cargo from one compartment of the cell to another. The AP-1 complex is composed of four subunits: γ, β1, μ1, and σ1. It is primarily associated with the trans-Golgi network and early endosomes, where it facilitates the sorting and packaging of cargo into vesicles for transport to various destinations within the cell. The AP-1 complex recognizes specific sorting signals on the membrane proteins and adaptor proteins, thereby ensuring the accurate delivery of cargo to the correct location. Defects in the AP-1 complex have been implicated in several human diseases, including neurological disorders and cancer.

Adaptor Protein Complex 2 (AP-2) is a protein complex that plays a crucial role in the formation of clathrin-coated vesicles, which are involved in intracellular trafficking and transport of membrane proteins and lipids. The AP-2 complex is composed of four subunits: alpha, beta, mu, and sigma, which form a heterotetrameric structure. It functions as a bridge between the clathrin lattice and the cytoplasmic domains of membrane proteins, such as transmembrane receptors, that are destined for endocytosis. The AP-2 complex recognizes specific sorting signals within the cytoplasmic tails of these membrane proteins, leading to their recruitment into forming clathrin-coated pits and subsequent internalization via clathrin-coated vesicles. This process is essential for various cellular functions, including receptor-mediated endocytosis, synaptic vesicle recycling, and membrane protein trafficking.

Adaptor Protein Complex 4 (AP-4) is a group of proteins that form a complex and play a crucial role in the intracellular trafficking of membrane proteins within eukaryotic cells. The AP-4 complex is composed of four subunits, namely, α-Adaptin, β2-Adaptin, Mu-Adaptin, and Sigmal-Adaptin4 (σ4A or σ4B).

The primary function of the AP-4 complex is to facilitate the sorting of proteins in the trans-Golgi network (TGN) and endosomes. It recognizes specific sorting signals present on the cytoplasmic tails of membrane proteins, recruits accessory proteins, and mediates the formation of transport vesicles that carry these proteins to their target destinations.

Mutations in genes encoding AP-4 complex subunits have been associated with several neurological disorders, including hereditary spastic paraplegia (HSP), mental retardation, and cerebral palsy. These genetic defects disrupt the normal functioning of the AP-4 complex, leading to aberrant protein trafficking and impaired neuronal development and function.

Adaptor protein complex subunits are proteins that combine to form adaptor protein complexes, which are essential components of intracellular transport vesicles. These complexes play a crucial role in recognizing and binding to specific cargo molecules, as well as interacting with coat proteins and membrane phospholipids to facilitate the formation and budding of transport vesicles from donor membranes.

There are five types of adaptor protein complexes, each consisting of several subunits: AP-1, AP-2, AP-3, AP-4, and AP-5. These subunits are named according to their molecular weights and the type of complex they form. For example, AP-1 consists of four subunits, including two large subunits (γ and β1 or β2), one medium subunit (μ1), and one small subunit (σ1).

The specific combination of subunits in each complex determines its function and localization within the cell. For instance, AP-1 is primarily involved in transport between the trans-Golgi network and endosomes, while AP-2 is responsible for clathrin-mediated endocytosis at the plasma membrane. Mutations in adaptor protein complex subunits have been linked to various human diseases, including neurological disorders and cancer.

Adaptor Protein Complex delta Subunits, also known as AP-4 complex, is a type of protein complex that plays a role in intracellular trafficking, specifically in the sorting and transport of proteins between the Golgi apparatus and endosomes. The AP-4 complex is composed of four subunits: beta-1, beta-2, gamma, and delta, with the delta subunit being one of its essential components.

The delta subunit of the AP-4 complex is encoded by the gene AP4D1 and is involved in the recognition and binding of specific sorting signals on protein cargo. Mutations in the AP4D1 gene have been associated with certain neurological disorders, such as hereditary spastic paraplegia and intellectual disability, highlighting the importance of this protein complex in proper brain function.

The adaptor protein complex mu (AP-μ or AP-2) is a heterotetrameric complex that plays a crucial role in clathrin-mediated endocytosis, a process by which cells internalize various molecules from their external environment. The subunits of the AP-μ complex are:

1. AP2M1 (Adaptin-μ1): This is the μ subunit, which binds to the clathrin heavy chain and helps recruit it to the membrane during vesicle formation. It also plays a role in cargo recognition by interacting with sorting signals on transmembrane proteins.
2. AP2B1 (Adaptin-β1): This is the β subunit, which interacts with the μ and σ subunits to form the core of the complex. It also binds to accessory proteins that regulate endocytosis.
3. AP2S1 (Adaptin-σ1): This is the σ subunit, which helps stabilize the interaction between the μ and β subunits and contributes to cargo recognition by binding to specific sorting signals on transmembrane proteins.
4. AP2L1 (Adaptin-λ1): This is the λ subunit, which interacts with the α subunit of adaptor protein complex 1 (AP-1) and helps coordinate the trafficking of proteins between different endocytic compartments.

Together, these subunits form a complex that plays a central role in clathrin-mediated endocytosis by regulating the recruitment of clathrin and other accessory proteins to the membrane, as well as the recognition and sorting of cargo molecules for internalization.

Adaptor proteins play a crucial role in vesicular transport, which is the process by which materials are transported within cells in membrane-bound sacs called vesicles. These adaptor proteins serve as a bridge between vesicle membranes and cytoskeletal elements or other cellular structures, facilitating the movement of vesicles throughout the cell.

There are several different types of adaptor proteins involved in vesicular transport, each with specific functions and localizations within the cell. Some examples include:

1. Clathrin Adaptor Protein Complex (AP-1, AP-2, AP-3, AP-4): These complexes are responsible for recruiting clathrin to membranes during vesicle formation, which helps to shape and stabilize the vesicle. They also play a role in sorting cargo into specific vesicles.

2. Coat Protein Complex I (COPI): This complex is involved in the transport of proteins between the endoplasmic reticulum (ER) and the Golgi apparatus, as well as within the Golgi itself. COPI-coated vesicles are formed by the assembly of coatomer proteins around the membrane, which helps to deform the membrane into a vesicle shape.

3. Coat Protein Complex II (COPII): This complex is involved in the transport of proteins from the ER to the Golgi apparatus. COPII-coated vesicles are formed by the assembly of Sar1, Sec23/24, and Sec13/31 proteins around the membrane, which helps to select cargo and form a vesicle.

4. BAR (Bin/Amphiphysin/Rvs) Domain Proteins: These proteins are involved in shaping and stabilizing membranes during vesicle formation. They can sense and curve membranes, recruiting other proteins to help form the vesicle.

5. SNARE Proteins: While not strictly adaptor proteins, SNAREs play a critical role in vesicle fusion by forming complexes that bring the vesicle and target membrane together. These complexes provide the energy required for membrane fusion, allowing for the release of cargo into the target compartment.

Overall, adaptor proteins are essential components of the cellular machinery that regulates intracellular trafficking. They help to select cargo, deform membranes, and facilitate vesicle formation, ensuring that proteins and lipids reach their correct destinations within the cell.

Adaptor Protein Complex (AP) gamma subunits are a part of the AP complexes, which are large protein assemblies involved in intracellular trafficking of proteins and vesicles. The AP complexes are responsible for recognizing specific sorting signals on membrane proteins and facilitating the formation of transport vesicles.

There are four different types of AP complexes (AP-1, AP-2, AP-3, and AP-4) that contain distinct subunit compositions. The gamma subunits are common to two of these complexes: AP-1 and AP-3.

AP-1 is primarily associated with transport between the Golgi apparatus and endosomes, while AP-3 is involved in trafficking from early endosomes to lysosomes or related organelles. The gamma subunit of AP-1 is called γ-adaptin, and the gamma subunit of AP-3 is called μ3A or μ3B, depending on the specific isoform.

Mutations in these gamma subunits can lead to various human genetic disorders, such as Hermansky-Pudlak syndrome (HPS) and X-linked mental retardation (XLMR).

Adaptor Protein Complex (AP) beta subunits are structural proteins that play a crucial role in intracellular vesicle trafficking. They are part of the heterotetrameric AP complex, which is responsible for recognizing and binding to specific sorting signals on membrane cargo proteins, allowing for their packaging into transport vesicles.

There are four different types of AP complexes (AP-1, AP-2, AP-3, and AP-4), each with a unique set of subunits that confer specific functions. The beta subunit is a common component of all four complexes and is essential for their stability and function.

The beta subunit interacts with other subunits within the AP complex as well as with accessory proteins, such as clathrin, to form a coat around the transport vesicle. This coat helps to shape the vesicle and facilitate its movement between different cellular compartments.

Mutations in genes encoding AP beta subunits have been linked to various human diseases, including forms of hemolytic anemia, neurological disorders, and immunodeficiency.

Adaptor proteins are a type of protein that play a crucial role in intracellular signaling pathways by serving as a link between different components of the signaling complex. Specifically, "signal transducing adaptor proteins" refer to those adaptor proteins that are involved in signal transduction processes, where they help to transmit signals from the cell surface receptors to various intracellular effectors. These proteins typically contain modular domains that allow them to interact with multiple partners, thereby facilitating the formation of large signaling complexes and enabling the integration of signals from different pathways.

Signal transducing adaptor proteins can be classified into several families based on their structural features, including the Src homology 2 (SH2) domain, the Src homology 3 (SH3) domain, and the phosphotyrosine-binding (PTB) domain. These domains enable the adaptor proteins to recognize and bind to specific motifs on other signaling molecules, such as receptor tyrosine kinases, G protein-coupled receptors, and cytokine receptors.

One well-known example of a signal transducing adaptor protein is the growth factor receptor-bound protein 2 (Grb2), which contains an SH2 domain that binds to phosphotyrosine residues on activated receptor tyrosine kinases. Grb2 also contains an SH3 domain that interacts with proline-rich motifs on other signaling proteins, such as the guanine nucleotide exchange factor SOS. This interaction facilitates the activation of the Ras small GTPase and downstream signaling pathways involved in cell growth, differentiation, and survival.

Overall, signal transducing adaptor proteins play a critical role in regulating various cellular processes by modulating intracellular signaling pathways in response to extracellular stimuli. Dysregulation of these proteins has been implicated in various diseases, including cancer and inflammatory disorders.

Clathrin is a type of protein that plays a crucial role in the formation of coated vesicles within cells. These vesicles are responsible for transporting materials between different cellular compartments, such as from the plasma membrane to the endoplasmic reticulum or Golgi apparatus. Clathrin molecules form a lattice-like structure that curves around the vesicle, providing stability and shape to the coated vesicle. This process is known as clathrin-mediated endocytosis.

The formation of clathrin-coated vesicles begins with the recruitment of clathrin proteins to specific sites on the membrane, where they assemble into a polygonal lattice structure. As more clathrin molecules join the assembly, the lattice curves and eventually pinches off from the membrane, forming a closed vesicle. The clathrin coat then disassembles, releasing the vesicle to continue with its intracellular transport mission.

Disruptions in clathrin-mediated endocytosis can lead to various cellular dysfunctions and diseases, including neurodegenerative disorders and certain types of cancer.

I'm sorry for any confusion, but "human characteristics" is not a medical term or concept. It refers to the typical traits, attributes, and features that define humans as a species, both physically and behaviorally. Physical human characteristics include bipedal locomotion, large brains, and fine motor skills, while behavioral characteristics can include complex language use, self-awareness, and sociality.

However, if you have any specific medical or health-related questions, I would be happy to help answer them to the best of my ability!

Monomeric Clathrin Assembly Proteins (also known as Clathrin Terminal Domain Proteins or CTD proteins) refer to a group of proteins that play a crucial role in the assembly and disassembly of clathrin-coated vesicles, which are involved in intracellular trafficking processes such as endocytosis and recycling of membrane receptors.

Clathrin is a triskelion-shaped protein made up of three heavy chains and three light chains. The monomeric clathrin assembly proteins, including CTD-associated proteins (CAPs) and serine kinases such as Clathrin Kinase (CLK), interact with the terminal domains of clathrin's heavy chains to regulate the formation and stability of clathrin lattices.

These proteins facilitate the self-assembly of clathrin molecules into polyhedral cages, which then deform the membrane and form vesicles that bud off from the plasma membrane or intracellular organelles. The monomeric clathrin assembly proteins also play a role in regulating the disassembly of these structures during the uncoating process, allowing for the recycling of clathrin molecules and the release of cargo.

In summary, Monomeric Clathrin Assembly Proteins are essential components of the clathrin-mediated trafficking pathway, facilitating the formation, stability, and disassembly of clathrin-coated vesicles.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

A protein subunit refers to a distinct and independently folding polypeptide chain that makes up a larger protein complex. Proteins are often composed of multiple subunits, which can be identical or different, that come together to form the functional unit of the protein. These subunits can interact with each other through non-covalent interactions such as hydrogen bonds, ionic bonds, and van der Waals forces, as well as covalent bonds like disulfide bridges. The arrangement and interaction of these subunits contribute to the overall structure and function of the protein.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

The GRB2 (Growth Factor Receptor-Bound Protein 2) adaptor protein is a cytoplasmic signaling molecule that plays a crucial role in intracellular signal transduction pathways, particularly those involved in cell growth, differentiation, and survival. It acts as a molecular adapter or scaffold, facilitating the interaction between various proteins to form multi-protein complexes and propagate signals from activated receptor tyrosine kinases (RTKs) to downstream effectors.

GRB2 contains several functional domains, including an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The SH2 domain is responsible for binding to specific phosphotyrosine residues on activated RTKs or other adaptor proteins, while the SH3 domains mediate interactions with proline-rich sequences in partner proteins.

Once GRB2 binds to an activated RTK, it recruits and activates the guanine nucleotide exchange factor SOS (Son of Sevenless), which in turn activates the RAS GTPase. Activated RAS then initiates a signaling cascade involving various kinases such as Raf, MEK, and ERK, ultimately leading to changes in gene expression and cellular responses.

In summary, GRB2 is an essential adaptor protein that facilitates the transmission of signals from activated growth factor receptors to downstream effectors, playing a critical role in regulating various cellular processes.

SHC (Src homology 2 domain containing) signaling adaptor proteins are a family of intracellular signaling molecules that play a crucial role in the transduction of signals from various cell surface receptors, including receptor tyrosine kinases (RTKs). These proteins contain several conserved domains, including Src homology 2 (SH2) and phosphotyrosine-binding (PTB) domains, which enable them to bind to specific phosphorylated tyrosine residues on activated receptors or other signaling molecules.

Once bound to the activated receptor, SHC proteins recruit and interact with various downstream signaling proteins, such as growth factor receptor-bound protein 2 (Grb2) and son of sevenless (SOS), thereby initiating intracellular signaling cascades that ultimately regulate diverse cellular processes, including proliferation, differentiation, survival, and migration. There are three main isoforms of SHC proteins in humans: p66Shc, p52Shc, and p46Shc, which differ in their structural organization and functional properties.

Abnormal regulation of SHC signaling adaptor proteins has been implicated in various pathological conditions, including cancer, diabetes, and neurodegenerative diseases. Therefore, understanding the molecular mechanisms underlying SHC-mediated signaling pathways may provide valuable insights into the development of novel therapeutic strategies for these disorders.

Adaptor protein complex (AP) sigma subunits are essential components of the AP complexes, which are large heterotetrameric protein assemblies involved in intracellular trafficking of proteins and vesicles. The AP complexes are responsible for recognizing specific sorting signals on membrane proteins and cargo, facilitating the formation and targeting of transport vesicles within the cell.

There are four main types of AP complexes (AP-1, AP-2, AP-3, and AP-4), each containing two large (~100 kDa) subunits, one medium (~50 kDa) subunit, and one small sigma (~20 kDa) subunit. The sigma subunit is responsible for recognizing and binding to specific sorting signals on the cytoplasmic tails of transmembrane proteins, thereby ensuring the proper sorting and targeting of these proteins during intracellular trafficking.

The sigma subunits share a conserved structural motif known as the σ2 domain, which is responsible for binding to the sorting signals on membrane proteins. The specificity of each AP complex for different sorting signals and membrane compartments is determined in part by the identity of its sigma subunit.

In summary, Adaptor protein complex (AP) sigma subunits are essential components of intracellular trafficking machinery that recognize and bind to specific sorting signals on membrane proteins, ensuring proper targeting and sorting of these proteins during vesicle formation and transport.

Endocytosis is the process by which cells absorb substances from their external environment by engulfing them in membrane-bound structures, resulting in the formation of intracellular vesicles. This mechanism allows cells to take up large molecules, such as proteins and lipids, as well as small particles, like bacteria and viruses. There are two main types of endocytosis: phagocytosis (cell eating) and pinocytosis (cell drinking). Phagocytosis involves the engulfment of solid particles, while pinocytosis deals with the uptake of fluids and dissolved substances. Other specialized forms of endocytosis include receptor-mediated endocytosis and caveolae-mediated endocytosis, which allow for the specific internalization of molecules through the interaction with cell surface receptors.

Membrane proteins are a type of protein that are embedded in the lipid bilayer of biological membranes, such as the plasma membrane of cells or the inner membrane of mitochondria. These proteins play crucial roles in various cellular processes, including:

1. Cell-cell recognition and signaling
2. Transport of molecules across the membrane (selective permeability)
3. Enzymatic reactions at the membrane surface
4. Energy transduction and conversion
5. Mechanosensation and signal transduction

Membrane proteins can be classified into two main categories: integral membrane proteins, which are permanently associated with the lipid bilayer, and peripheral membrane proteins, which are temporarily or loosely attached to the membrane surface. Integral membrane proteins can further be divided into three subcategories based on their topology:

1. Transmembrane proteins, which span the entire width of the lipid bilayer with one or more alpha-helices or beta-barrels.
2. Lipid-anchored proteins, which are covalently attached to lipids in the membrane via a glycosylphosphatidylinositol (GPI) anchor or other lipid modifications.
3. Monotopic proteins, which are partially embedded in the membrane and have one or more domains exposed to either side of the bilayer.

Membrane proteins are essential for maintaining cellular homeostasis and are targets for various therapeutic interventions, including drug development and gene therapy. However, their structural complexity and hydrophobicity make them challenging to study using traditional biochemical methods, requiring specialized techniques such as X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and single-particle cryo-electron microscopy (cryo-EM).

Coated vesicles are membrane-bound compartments found within cells that are characterized by a coat of proteins on their cytoplasmic surface. These vesicles play a crucial role in intracellular transport and membrane trafficking, particularly in the process of endocytosis and exocytosis.

Endocytosis is the process by which cells engulf extracellular material, such as nutrients or molecules like receptors, into vesicles that are formed from the plasma membrane. During this process, coated vesicles called clathrin-coated vesicles form around the region of the plasma membrane where endocytosis is taking place. Clathrin, a protein involved in the formation of these vesicles, polymerizes to form a lattice-like structure that curves the membrane into a spherical shape and pinches it off from the plasma membrane.

Exocytosis, on the other hand, is the process by which cells release molecules or vesicles containing molecules to the extracellular space. In this case, coated vesicles called COP-coated vesicles are involved. These vesicles have a different protein coat, composed of coatomer proteins (COP), and they mediate the transport of proteins and lipids between the endoplasmic reticulum, Golgi apparatus, and the plasma membrane.

Coated vesicles are essential for maintaining cellular homeostasis by controlling the movement of molecules in and out of the cell, as well as the proper sorting and targeting of proteins within the cell. Dysfunctions in coated vesicle formation or trafficking have been implicated in various diseases, including neurodegenerative disorders and cancer.

Protein transport, in the context of cellular biology, refers to the process by which proteins are actively moved from one location to another within or between cells. This is a crucial mechanism for maintaining proper cell function and regulation.

Intracellular protein transport involves the movement of proteins within a single cell. Proteins can be transported across membranes (such as the nuclear envelope, endoplasmic reticulum, Golgi apparatus, or plasma membrane) via specialized transport systems like vesicles and transport channels.

Intercellular protein transport refers to the movement of proteins from one cell to another, often facilitated by exocytosis (release of proteins in vesicles) and endocytosis (uptake of extracellular substances via membrane-bound vesicles). This is essential for communication between cells, immune response, and other physiological processes.

It's important to note that any disruption in protein transport can lead to various diseases, including neurological disorders, cancer, and metabolic conditions.

The trans-Golgi network (TGN) is a structure in the cell's endomembrane system that is involved in the sorting and distribution of proteins and lipids to their final destinations within the cell or for secretion. It is a part of the Golgi apparatus, which consists of a series of flattened, membrane-bound sacs called cisternae. The TGN is located at the trans face (or "exit" side) of the Golgi complex and is the final stop for proteins that have been modified as they pass through the Golgi stacks.

At the TGN, proteins are sorted into different transport vesicles based on their specific targeting signals. These vesicles then bud off from the TGN and move to their respective destinations, such as endosomes, lysosomes, the plasma membrane, or secretory vesicles for exocytosis. The TGN also plays a role in the modification of lipids and the formation of primary lysosomes.

In summary, the trans-Golgi network is a crucial sorting and distribution center within the cell that ensures proteins and lipids reach their correct destinations to maintain proper cellular function.

Clathrin-coated vesicles are small, membrane-bound structures that play a crucial role in intracellular transport within eukaryotic cells. They are formed by the coating of the plasma membrane or the membranes of other organelles with a lattice-like structure made up of clathrin proteins.

The formation of clathrin-coated vesicles is initiated when adaptor proteins recognize and bind to specific signals on the cytoplasmic side of the membrane. These adaptor proteins then recruit clathrin molecules, which assemble into a cage-like structure that deforms the membrane into a spherical shape. The vesicle then pinches off from the membrane, enclosed in its clathrin coat.

Once formed, clathrin-coated vesicles can transport proteins and other molecules between different cellular compartments, such as from the plasma membrane to endosomes or from the Golgi apparatus to the endoplasmic reticulum. The clathrin coat is subsequently disassembled, allowing the vesicle to fuse with its target membrane and release its contents.

Defects in clathrin-coated vesicle function have been implicated in a variety of human diseases, including neurodegenerative disorders and certain forms of cancer.

Endosomes are membrane-bound compartments within eukaryotic cells that play a critical role in intracellular trafficking and sorting of various cargoes, including proteins and lipids. They are formed by the invagination of the plasma membrane during endocytosis, resulting in the internalization of extracellular material and cell surface receptors.

Endosomes can be classified into early endosomes, late endosomes, and recycling endosomes based on their morphology, molecular markers, and functional properties. Early endosomes are the initial sorting stations for internalized cargoes, where they undergo sorting and processing before being directed to their final destinations. Late endosomes are more acidic compartments that mature from early endosomes and are responsible for the transport of cargoes to lysosomes for degradation.

Recycling endosomes, on the other hand, are involved in the recycling of internalized cargoes back to the plasma membrane or to other cellular compartments. Endosomal sorting and trafficking are regulated by a complex network of molecular interactions involving various proteins, lipids, and intracellular signaling pathways.

Defects in endosomal function have been implicated in various human diseases, including neurodegenerative disorders, developmental abnormalities, and cancer. Therefore, understanding the mechanisms underlying endosomal trafficking and sorting is of great importance for developing therapeutic strategies to treat these conditions.

Carrier proteins, also known as transport proteins, are a type of protein that facilitates the movement of molecules across cell membranes. They are responsible for the selective and active transport of ions, sugars, amino acids, and other molecules from one side of the membrane to the other, against their concentration gradient. This process requires energy, usually in the form of ATP (adenosine triphosphate).

Carrier proteins have a specific binding site for the molecule they transport, and undergo conformational changes upon binding, which allows them to move the molecule across the membrane. Once the molecule has been transported, the carrier protein returns to its original conformation, ready to bind and transport another molecule.

Carrier proteins play a crucial role in maintaining the balance of ions and other molecules inside and outside of cells, and are essential for many physiological processes, including nerve impulse transmission, muscle contraction, and nutrient uptake.

Recombinant fusion proteins are artificially created biomolecules that combine the functional domains or properties of two or more different proteins into a single protein entity. They are generated through recombinant DNA technology, where the genes encoding the desired protein domains are linked together and expressed as a single, chimeric gene in a host organism, such as bacteria, yeast, or mammalian cells.

The resulting fusion protein retains the functional properties of its individual constituent proteins, allowing for novel applications in research, diagnostics, and therapeutics. For instance, recombinant fusion proteins can be designed to enhance protein stability, solubility, or immunogenicity, making them valuable tools for studying protein-protein interactions, developing targeted therapies, or generating vaccines against infectious diseases or cancer.

Examples of recombinant fusion proteins include:

1. Etaglunatide (ABT-523): A soluble Fc fusion protein that combines the heavy chain fragment crystallizable region (Fc) of an immunoglobulin with the extracellular domain of the human interleukin-6 receptor (IL-6R). This fusion protein functions as a decoy receptor, neutralizing IL-6 and its downstream signaling pathways in rheumatoid arthritis.
2. Etanercept (Enbrel): A soluble TNF receptor p75 Fc fusion protein that binds to tumor necrosis factor-alpha (TNF-α) and inhibits its proinflammatory activity, making it a valuable therapeutic option for treating autoimmune diseases like rheumatoid arthritis, ankylosing spondylitis, and psoriasis.
3. Abatacept (Orencia): A fusion protein consisting of the extracellular domain of cytotoxic T-lymphocyte antigen 4 (CTLA-4) linked to the Fc region of an immunoglobulin, which downregulates T-cell activation and proliferation in autoimmune diseases like rheumatoid arthritis.
4. Belimumab (Benlysta): A monoclonal antibody that targets B-lymphocyte stimulator (BLyS) protein, preventing its interaction with the B-cell surface receptor and inhibiting B-cell activation in systemic lupus erythematosus (SLE).
5. Romiplostim (Nplate): A fusion protein consisting of a thrombopoietin receptor agonist peptide linked to an immunoglobulin Fc region, which stimulates platelet production in patients with chronic immune thrombocytopenia (ITP).
6. Darbepoetin alfa (Aranesp): A hyperglycosylated erythropoiesis-stimulating protein that functions as a longer-acting form of recombinant human erythropoietin, used to treat anemia in patients with chronic kidney disease or cancer.
7. Palivizumab (Synagis): A monoclonal antibody directed against the F protein of respiratory syncytial virus (RSV), which prevents RSV infection and is administered prophylactically to high-risk infants during the RSV season.
8. Ranibizumab (Lucentis): A recombinant humanized monoclonal antibody fragment that binds and inhibits vascular endothelial growth factor A (VEGF-A), used in the treatment of age-related macular degeneration, diabetic retinopathy, and other ocular disorders.
9. Cetuximab (Erbitux): A chimeric monoclonal antibody that binds to epidermal growth factor receptor (EGFR), used in the treatment of colorectal cancer and head and neck squamous cell carcinoma.
10. Adalimumab (Humira): A fully humanized monoclonal antibody that targets tumor necrosis factor-alpha (TNF-α), used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriasis, and Crohn's disease.
11. Bevacizumab (Avastin): A recombinant humanized monoclonal antibody that binds to VEGF-A, used in the treatment of various cancers, including colorectal, lung, breast, and kidney cancer.
12. Trastuzumab (Herceptin): A humanized monoclonal antibody that targets HER2/neu receptor, used in the treatment of breast cancer.
13. Rituximab (Rituxan): A chimeric monoclonal antibody that binds to CD20 antigen on B cells, used in the treatment of non-Hodgkin's lymphoma and rheumatoid arthritis.
14. Palivizumab (Synagis): A humanized monoclonal antibody that binds to the F protein of respiratory syncytial virus, used in the prevention of respiratory syncytial virus infection in high-risk infants.
15. Infliximab (Remicade): A chimeric monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including Crohn's disease, ulcerative colitis, rheumatoid arthritis, and ankylosing spondylitis.
16. Natalizumab (Tysabri): A humanized monoclonal antibody that binds to α4β1 integrin, used in the treatment of multiple sclerosis and Crohn's disease.
17. Adalimumab (Humira): A fully human monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, Crohn's disease, and ulcerative colitis.
18. Golimumab (Simponi): A fully human monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and ulcerative colitis.
19. Certolizumab pegol (Cimzia): A PEGylated Fab' fragment of a humanized monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and Crohn's disease.
20. Ustekinumab (Stelara): A fully human monoclonal antibody that targets IL-12 and IL-23, used in the treatment of psoriasis, psoriatic arthritis, and Crohn's disease.
21. Secukinumab (Cosentyx): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis, psoriatic arthritis, and ankylosing spondylitis.
22. Ixekizumab (Taltz): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis and psoriatic arthritis.
23. Brodalumab (Siliq): A fully human monoclonal antibody that targets IL-17 receptor A, used in the treatment of psoriasis.
24. Sarilumab (Kevzara): A fully human monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis.
25. Tocilizumab (Actemra): A humanized monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis, systemic juvenile idiopathic arthritis, polyarticular juvenile idiopathic arthritis, giant cell arteritis, and chimeric antigen receptor T-cell-induced cytokine release syndrome.
26. Siltuximab (Sylvant): A chimeric monoclonal antibody that targets IL-6, used in the treatment of multicentric Castleman disease.
27. Satralizumab (Enspryng): A humanized monoclonal antibody that targets IL-6 receptor alpha, used in the treatment of neuromyelitis optica spectrum disorder.
28. Sirukumab (Plivensia): A human monoclonal antibody that targets IL-6, used in the treatment

A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.

Macromolecular substances, also known as macromolecules, are large, complex molecules made up of repeating subunits called monomers. These substances are formed through polymerization, a process in which many small molecules combine to form a larger one. Macromolecular substances can be naturally occurring, such as proteins, DNA, and carbohydrates, or synthetic, such as plastics and synthetic fibers.

In the context of medicine, macromolecular substances are often used in the development of drugs and medical devices. For example, some drugs are designed to bind to specific macromolecules in the body, such as proteins or DNA, in order to alter their function and produce a therapeutic effect. Additionally, macromolecular substances may be used in the creation of medical implants, such as artificial joints and heart valves, due to their strength and durability.

It is important for healthcare professionals to have an understanding of macromolecular substances and how they function in the body, as this knowledge can inform the development and use of medical treatments.

Signal transduction is the process by which a cell converts an extracellular signal, such as a hormone or neurotransmitter, into an intracellular response. This involves a series of molecular events that transmit the signal from the cell surface to the interior of the cell, ultimately resulting in changes in gene expression, protein activity, or metabolism.

The process typically begins with the binding of the extracellular signal to a receptor located on the cell membrane. This binding event activates the receptor, which then triggers a cascade of intracellular signaling molecules, such as second messengers, protein kinases, and ion channels. These molecules amplify and propagate the signal, ultimately leading to the activation or inhibition of specific cellular responses.

Signal transduction pathways are highly regulated and can be modulated by various factors, including other signaling molecules, post-translational modifications, and feedback mechanisms. Dysregulation of these pathways has been implicated in a variety of diseases, including cancer, diabetes, and neurological disorders.

Phosphoproteins are proteins that have been post-translationally modified by the addition of a phosphate group (-PO3H2) onto specific amino acid residues, most commonly serine, threonine, or tyrosine. This process is known as phosphorylation and is mediated by enzymes called kinases. Phosphoproteins play crucial roles in various cellular processes such as signal transduction, cell cycle regulation, metabolism, and gene expression. The addition or removal of a phosphate group can activate or inhibit the function of a protein, thereby serving as a switch to control its activity. Phosphoproteins can be detected and quantified using techniques such as Western blotting, mass spectrometry, and immunofluorescence.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

Transport vesicles are membrane-bound sacs or containers within cells that are responsible for the intracellular transport of proteins, lipids, and other cargo. These vesicles form when a portion of a donor membrane buds off, enclosing the cargo inside. There are different types of transport vesicles, including:

1. Endoplasmic reticulum (ER) vesicles: These vesicles form from the ER and transport proteins to the Golgi apparatus for further processing.
2. Golgi-derived vesicles: After proteins have been processed in the Golgi, they are packaged into transport vesicles that can deliver them to their final destinations within the cell or to the plasma membrane for secretion.
3. Endocytic vesicles: These vesicles form when a portion of the plasma membrane invaginates and pinches off, engulfing extracellular material or fluid. Examples include clathrin-coated vesicles and caveolae.
4. Lysosomal vesicles: These vesicles transport materials to lysosomes for degradation.
5. Secretory vesicles: These vesicles store proteins and other molecules that will be secreted from the cell. When stimulated, these vesicles fuse with the plasma membrane, releasing their contents to the extracellular space.

GTP-binding protein (G protein) alpha subunits are a family of proteins that play a crucial role in cell signaling pathways, particularly those involved in the transmission of signals across the plasma membrane in response to hormones, neurotransmitters, and other extracellular signals. These proteins bind to guanosine triphosphate (GTP) and undergo conformational changes upon activation, which enables them to interact with downstream effectors and modulate various cellular responses.

There are several classes of G protein alpha subunits, including Gs, Gi/o, Gq/11, and G12/13, each of which activates distinct signaling cascades upon activation. For instance, Gs alpha subunits activate adenylyl cyclase, leading to increased levels of cAMP and the activation of protein kinase A (PKA), while Gi/o alpha subunits inhibit adenylyl cyclase and reduce cAMP levels. Gq/11 alpha subunits activate phospholipase C-beta (PLC-β), which leads to the production of inositol trisphosphate (IP3) and diacylglycerol (DAG), while G12/13 alpha subunits modulate cytoskeletal rearrangements through activation of Rho GTPases.

Mutations in G protein alpha subunits have been implicated in various human diseases, including cancer, neurological disorders, and cardiovascular disease. Therefore, understanding the structure, function, and regulation of these proteins is essential for developing novel therapeutic strategies to target these conditions.

A cell membrane, also known as the plasma membrane, is a thin semi-permeable phospholipid bilayer that surrounds all cells in animals, plants, and microorganisms. It functions as a barrier to control the movement of substances in and out of the cell, allowing necessary molecules such as nutrients, oxygen, and signaling molecules to enter while keeping out harmful substances and waste products. The cell membrane is composed mainly of phospholipids, which have hydrophilic (water-loving) heads and hydrophobic (water-fearing) tails. This unique structure allows the membrane to be flexible and fluid, yet selectively permeable. Additionally, various proteins are embedded in the membrane that serve as channels, pumps, receptors, and enzymes, contributing to the cell's overall functionality and communication with its environment.

GTP-binding proteins, also known as G proteins, are a family of molecular switches present in many organisms, including humans. They play a crucial role in signal transduction pathways, particularly those involved in cellular responses to external stimuli such as hormones, neurotransmitters, and sensory signals like light and odorants.

G proteins are composed of three subunits: α, β, and γ. The α-subunit binds GTP (guanosine triphosphate) and acts as the active component of the complex. When a G protein-coupled receptor (GPCR) is activated by an external signal, it triggers a conformational change in the associated G protein, allowing the α-subunit to exchange GDP (guanosine diphosphate) for GTP. This activation leads to dissociation of the G protein complex into the GTP-bound α-subunit and the βγ-subunit pair. Both the α-GTP and βγ subunits can then interact with downstream effectors, such as enzymes or ion channels, to propagate and amplify the signal within the cell.

The intrinsic GTPase activity of the α-subunit eventually hydrolyzes the bound GTP to GDP, which leads to re-association of the α and βγ subunits and termination of the signal. This cycle of activation and inactivation makes G proteins versatile signaling elements that can respond quickly and precisely to changing environmental conditions.

Defects in G protein-mediated signaling pathways have been implicated in various diseases, including cancer, neurological disorders, and cardiovascular diseases. Therefore, understanding the function and regulation of GTP-binding proteins is essential for developing targeted therapeutic strategies.

Coated pits are specialized regions on the cell membrane that are involved in the process of endocytosis. They are called "coated" pits because they are covered or coated with a layer of proteins and clathrin molecules, which form a lattice-like structure that helps to shape and invaginate the membrane inward, forming a vesicle.

Coated pits play an important role in regulating cellular uptake of various substances, such as nutrients, hormones, and receptors. Once the coated pit has pinched off from the cell membrane, it becomes a coated vesicle, which can then fuse with other intracellular compartments to deliver its contents.

The formation of coated pits is a highly regulated process that involves the recruitment of specific proteins and adaptors to the site of endocytosis. Defects in this process have been implicated in various diseases, including neurodevelopmental disorders and cancer.

Transfection is a term used in molecular biology that refers to the process of deliberately introducing foreign genetic material (DNA, RNA or artificial gene constructs) into cells. This is typically done using chemical or physical methods, such as lipofection or electroporation. Transfection is widely used in research and medical settings for various purposes, including studying gene function, producing proteins, developing gene therapies, and creating genetically modified organisms. It's important to note that transfection is different from transduction, which is the process of introducing genetic material into cells using viruses as vectors.

Medical Definition of "Multiprotein Complexes" :

Multiprotein complexes are large molecular assemblies composed of two or more proteins that interact with each other to carry out specific cellular functions. These complexes can range from relatively simple dimers or trimers to massive structures containing hundreds of individual protein subunits. They are formed through a process known as protein-protein interaction, which is mediated by specialized regions on the protein surface called domains or motifs.

Multiprotein complexes play critical roles in many cellular processes, including signal transduction, gene regulation, DNA replication and repair, protein folding and degradation, and intracellular transport. The formation of these complexes is often dynamic and regulated in response to various stimuli, allowing for precise control of their function.

Disruption of multiprotein complexes can lead to a variety of diseases, including cancer, neurodegenerative disorders, and infectious diseases. Therefore, understanding the structure, composition, and regulation of these complexes is an important area of research in molecular biology and medicine.

I'm sorry for any confusion, but "GRB10 Adaptor Protein" does not have a specific medical definition as it is related to molecular biology and cellular signaling.

GRB10 (Growth Factor Receptor-Bound Protein 10) is an adaptor protein that plays a crucial role in intracellular signal transduction, particularly in the insulin signaling pathway. Adaptor proteins do not have enzymatic activity but instead facilitate the interaction and assembly of various signaling molecules to form complexes, thereby modulating the strength, duration, and specificity of cellular responses.

GRB10 adaptor protein functions as a negative regulator of insulin and insulin-like growth factor 1 (IGF-1) signaling by interacting with the insulin receptor substrate (IRS) proteins and inhibiting their tyrosine phosphorylation, which is essential for downstream signal transduction. Mutations in GRB10 have been associated with various metabolic disorders, such as diabetes and growth abnormalities.

While not a medical definition per se, I hope this information helps you better understand the role of the GRB10 adaptor protein in cellular signaling.

Tertiary protein structure refers to the three-dimensional arrangement of all the elements (polypeptide chains) of a single protein molecule. It is the highest level of structural organization and results from interactions between various side chains (R groups) of the amino acids that make up the protein. These interactions, which include hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges, give the protein its unique shape and stability, which in turn determines its function. The tertiary structure of a protein can be stabilized by various factors such as temperature, pH, and the presence of certain ions. Any changes in these factors can lead to denaturation, where the protein loses its tertiary structure and thus its function.

A "gene product" is a general term that refers to the biochemical material or molecule produced by a gene after it has been transcribed and translated. This can include proteins, RNA molecules, or other types of functional genetic material.

In the context of "nef," this refers to a specific protein encoded by the nef gene found in the human immunodeficiency virus (HIV), which causes AIDS. The nef gene is one of the nine genes present in the HIV genome, and it encodes for a protein that plays a crucial role in the viral replication cycle and the pathogenesis of HIV infection.

The nef protein has multiple functions, including downregulation of CD4 receptors on the surface of infected cells, which helps the virus evade the immune response. It also enhances viral infectivity and modulates various cell signaling pathways to promote viral replication and survival. The nef gene product is an important target for HIV research and potential therapeutic interventions.

"Entrez Gene: AP2A2 adaptor-related protein complex 2, alpha 2 subunit". Chen H, Fre S, Slepnev VI, Capua MR, Takei K, Butler MH ... AP-2 complex subunit alpha-2 is a protein that in humans is encoded by the AP2A2 gene. AP2A2 has been shown to interact with ... Robinson MS (Mar 1989). "Cloning of cDNAs encoding two related 100-kD coated vesicle proteins (alpha-adaptins)". The Journal of ... the cytoplasmic domains of human and simian retroviral transmembrane proteins with components of the clathrin adaptor complexes ...
... either directly or through adaptor proteins. This gene encodes an alpha subunit of the heteromeric SEC61 complex, which also ... Protein transport protein Sec61 subunit alpha isoform 1 is a protein that in humans is encoded by the SEC61A1 gene. The protein ... "Entrez Gene: SEC61A1 Sec61 alpha 1 subunit (S. cerevisiae)". Wiertz EJ, Tortorella D, Bogyo M, et al. (1997). "Sec61-mediated ... 2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi: ...
This gene encodes a protein which interacts with clathrin and adaptor-related protein complex 2, alpha 1 subunit. The protein ... 1998). "Intersectin, a novel adaptor protein with two Eps15 homology and five Src homology 3 domains". J. Biol. Chem. 273 (47 ... 1997). "Binding specificity and in vivo targets of the EH domain, a novel protein-protein interaction module". Genes Dev. 11 ( ... "The epsins define a family of proteins that interact with components of the clathrin coat and contain a new protein module". J ...
This gene encodes the alpha 1 adaptin subunit of the adaptor protein 2 (AP2 adaptors) complex found in clathrin coated vesicles ... "Entrez Gene: AP2A1 adaptor-related protein complex 2, alpha 1 subunit". Nishimura, Takashi; Fukata Yuko; Kato Katsuhiro; ... Adaptor-related protein complex 2, alpha 1 has been shown to interact with DPYSL2 and NUMB. GRCh38: Ensembl release 89: ... AP-2 complex subunit alpha-1 is a protein that in humans is encoded by the AP2A1 gene. ...
... and some of the adapter proteins, such as talin, paxillin and tensin. Many of these focal complexes fail to mature and are ... Integrins are heterodimers which are formed from one beta and one alpha subunit. These subunits are present in different forms ... bind to and associate with this integrin-adapter protein-cytoskeleton complex, and this forms the basis of a focal adhesion. ... However, some focal complexes mature into larger and stable focal adhesions, and recruit many more proteins such as zyxin. ...
The family routinely lies on the clathrin adaptor complex 3 beta-1 subunit proteins. The exact function of DUF 1682 is unclear ... The C-terminal portion of the protein is highly charged and its secondary structure is predicted to be that of an alpha helix ... The final protein is thought to be translated from the endoplasmic reticulum into the cytoplasm of the cell. The protein is ... The portion of the protein which extends into the cytosol is predicted to be highly phosphorylated as the protein's ...
"Entrez Gene: AP2M1 adaptor-related protein complex 2, mu 1 subunit". Follows ER, McPheat JC, Minshull C, Moore NC, Pauptit RA, ... adaptor-receptor recognition and binding of alpha-adaptin subunits to the plasma membrane contribute to recruitment of adaptor ... AP-2 complex subunit mu is a protein that in humans is encoded by the AP2M1 gene. This gene encodes a subunit of the ... heterotetrameric coat assembly protein complex 2 (AP2), which belongs to the adaptor complexes medium subunits family. The ...
AP complexes are heterotetramers composed of two large subunits (adaptins), a medium subunit (mu) and a small subunit (sigma). ... For example, in AP1 these subunits are gamma-1-adaptin, beta-1-adaptin, mu-1 and sigma-1, while in AP2 they are alpha-adaptin, ... Adaptor protein (AP) complexes are found in coated vesicles and clathrin-coated pits. AP complexes connect cargo proteins and ... Touz MC, Kulakova L, Nash TE (July 2004). "Adaptor protein complex 1 mediates the transport of lysosomal proteins from a Golgi- ...
... proteins or receptors named A1 or Alpha-1 : Actin, alpha 1 Actinin, alpha 1 Adaptor-related protein complex 2, alpha 1 Aldehyde ... alpha 1 Proteasome (prosome, macropain) subunit, alpha 1 Protein kinase, AMP-activated, alpha 1 Protein tyrosine phosphatase, ... alpha 1 Gap junction protein, alpha 1 GDNF family receptor alpha 1 Glutathione S-transferase A1 Glycine receptor, alpha 1 Heat ... alpha 1 Major histocompatibility complex, class II, DP alpha 1 Major histocompatibility complex, class II, DQ alpha 1 Myosin ...
T-cell receptor alpha locus is a protein that in humans is encoded by the TRA gene, also known as TCRA or TRA@. It contributes ... "The implications of subunit interactions for the structure of the T cell receptor-CD3 complex". Eur. J. Immunol. 20 (2): 299- ... 2001). "The Transmembrane Adaptor Protein Trim Regulates T Cell Receptor (Tcr) Expression and Tcr-Mediated Signaling via an ... 2001). "Importance of the T cell receptor alpha-chain transmembrane distal region for assembly with cognate subunits". Mol. ...
The other large protein has different designations in the different complexes. In AP-1 it is named γ (gamma), AP-2 has α (alpha ... The two smaller proteins are a medium subunit named μ (mu ~50 kD) and a small subunit σ (sigma ~20 kD), and named 1 through 5 ... Most of the adaptor proteins are heterotetramers. In the AP complexes, there are two large proteins (~100 kD) and two smaller ... Vesicular transport adaptor proteins are proteins involved in forming complexes that function in the trafficking of molecules ...
... the plasma membrane the TCR receptor chains α and β associate with six additional adaptor proteins to form an octameric complex ... The TCR is a disulfide-linked membrane-anchored heterodimeric protein normally consisting of the highly variable alpha (α) and ... The two main subunits of TCR (α- and β-chains) are twisted together. CD3 and zeta subunits are required to carry out the signal ... LAT associates with another scaffolding protein Slp-76 via the Grap2 adaptor protein, which provides additional binding sites. ...
It is considered an extracellular matrix protein that functions as an adapter protein where the Matrilin-3 subunit can form ... It is considered the shortest and least complex member of the family, consisting of only one Von Willebrand Factor A domain, ... and an alpha-helical coiled-coil domain. Matrilin-3 does not contain the second vWFA -like domain that is present in the rest ... The Matrilin-3 protein is protein linked to the development of cartilage and bone, and consists of one Von Willebrand Factor A ...
AP (adaptor protein) complexes are found in coated vesicles and clathrin-coated pits. AP complexes connect cargo proteins and ... in AP1 these subunits are gamma-1-adaptin, beta-1-adaptin, mu-1 and sigma-1, while in AP2 they are alpha-adaptin, beta-2- ... The two major types of clathrin adaptor complexes are the heterotetrameric adaptor protein (AP) complexes, and the monomeric ... Touz MC, Kulakova L, Nash TE (July 2004). "Adaptor protein complex 1 mediates the transport of lysosomal proteins from a Golgi- ...
The protein encoded by this gene is a gamma-adaptin protein and it belongs to the adaptor complexes large subunits family. This ... The adaptin family of proteins is composed of four classes of molecules named alpha, beta-, beta prime- and gamma- adaptins. ... "Entrez Gene: AP1G2 adaptor-related protein complex 1, gamma 2 subunit". Rost, Martina; Döring Tatjana; Prange Reinhild (Nov ... AP-1 complex subunit gamma-like 2 is a protein that in humans is encoded by the AP1G2 gene. Adaptins are important components ...
The protein encoded by this gene is a gamma-adaptin protein and it belongs to the adaptor complexes large subunits family. Two ... The adaptin family of proteins is composed of four classes of molecules named alpha, beta-, beta prime- and gamma- adaptins. ... "Entrez Gene: AP1G1 adaptor-related protein complex 1, gamma 1 subunit". Fölsch H, Ohno H, Bonifacino JS, Mellman I (Oct 1999 ... "Similar subunit interactions contribute to assembly of clathrin adaptor complexes and COPI complex: analysis using yeast three- ...
... of rRNA processing Protein Phosphorylation Ribosomal small subunit biogenesis RIOK1 is the only component of the PRMT5 complex ... used as a basis for synthesis of a macrocyclic inhibitor of protein-protein interactions between PRMT5 and its adaptor proteins ... modifications the protein Kinase RIO1 has 2 phosphoserines in positions 21 and 22 Its secondary structure consist of 9 alpha ... 6:7,389,496-7,418,037) Effects on modified protein - protein degradation, triggered by K411-m1; protein stabilization, ...
All ATP-dependent chromatin-remodeling complexes possess a sub unit of ATPase that belongs to the SNF2 superfamily of proteins ... hADA3 may act as an adaptor protein linking transcription factors with other HAT complexes. In the absence of hADA3, TP53 ... factor implicated in the tumorigenesis and progression of breast cancer via its binding to the estrogen receptor alpha (ERα). ... ATP-dependent chromatin remodeling complexes. Specific protein complexes, known as histone-modifying complexes catalyze ...
The coatomer protein complex is made up of seven nonidentical protein subunits. These seven nonidentical protein subunits are ... allowing it to insert an amphipathic alpha helix into the lipid bilayer of the Golgi complex. Next, the ARF1 protein recruits ... Coatomers are functionally analogous and evolutionarily homologous to clathrin adaptor proteins, also known as adaptins, which ... The Sar1-GTP and Sec23-24 complex recruits another protein complex called Sec13/Sec31. This complex polymerizes to form the ...
AP1S2: AP-1 complex subunit sigma-2. Adaptor protein complex 1 is found on the cytoplasmic face of vesicles located at the ... GDI1: RabGDI alpha makes a complex with geranylgeranylated small GTP-binding proteins of the Rab family and keeps them in the ... "AP1S2 adaptor-related protein complex 1, sigma 2 subunit". Entrez Gene. National Center for Biotechnology Information, U.S. ... December 2006). "Mutations in the gene encoding the Sigma 2 subunit of the adaptor protein 1 complex, AP1S2, cause X-linked ...
... is an endocytic accessory protein that interacts with EPS15 (MIM 600051), the alpha subunit of the clathrin adaptor AP2 ( ... 2000). "Regulation of complex formation of POB1/epsin/adaptor protein complex 2 by mitotic phosphorylation". J. Biol. Chem. 275 ... Timsit YE, Miller SL, Mohney RP, O'Bryan JP (2005). "The U-box ligase carboxyl-terminus of Hsc 70-interacting protein ... Epsin-1 is a protein that in humans is encoded by the EPN1 gene. ... as well as with other accessory proteins for the endocytosis of ...
Each molecule of the dynein motor is a complex protein assembly composed of many smaller polypeptide subunits. Cytoplasmic and ... another multisubunit protein that is essential for mitosis, and a cargo adaptor. The tri-complex, which includes dynein, ... One attached alpha-helix from the stalk is pulled by the buttress, sliding the helix half a heptad repeat relative to its ... The dynactin complex is composed of more than 20 subunits, of which p150(Glued) is the largest. There is no definitive evidence ...
"Entrez Gene: AP3B2 adaptor-related protein complex 3, beta 2 subunit". Human AP3B2 genome location and AP3B2 gene details page ... Dubois T, Zemlickova E, Howell S, Aitken A (2003). "Centaurin-alpha 1 associates in vitro and in vivo with nucleolin". Biochem ... AP-3 complex subunit beta-2 is a protein that in humans is encoded by the AP3B2 gene. GRCm38: Ensembl release 89: ... 1997). "AP-3: an adaptor-like protein complex with ubiquitous expression". EMBO J. 16 (5): 917-28. doi:10.1093/emboj/16.5.917. ...
In contrast to IL-31RA, which binds SHP-2, the OSMR interacts with the adaptor protein Shc via the phosphorylated tyrosines on ... IL-31 signals via a receptor complex that is composed of IL-31 receptor A (IL31RA) and oncostatin M receptor (OSMR) subunits. ... The receptor for IL-31 is a heterodimer of the interleukin 31 receptor alpha (IL-31RA) and OSMR. IL-31RA was originally ... These receptor subunits are expressed in activated monocytes and in unstimulated epithelial cells. IL-31RA binds IL-31 through ...
... encoding protein Serine incorporator 3 SHLD1: encoding protein Shieldin complex subunit 1 SLC17A9: encoding protein Solute ... encoding protein Transmembrane prostate androgen-induced protein TTPAL: encoding protein Tocopherol (alpha) transfer protein- ... encoding protein Kizuna centrosomal protein Kua-UEV: LIME1: encoding protein Lck-interacting transmembrane adapter 1 LZTS3: ... encoding protein Zinc finger protein 334 ZNF343: encoding protein Zinc finger protein 343 ZSWIM3: encoding protein Zinc finger ...
... s feature prominently in the proteins making up the nuclear pore complex (NPC); alpha solenoid and beta propeller ... and its adaptor protein importin alpha is an alpha solenoid formed from Armadillo repeats. Transporters of other molecules, ... For example, regulatory subunit A (also known as PR65) of protein phosphatase 2A is a HEAT-repeat alpha solenoid whose ... "alpha alpha superhelix". The CATH database uses the term "alpha horseshoe" for these proteins, and uses "alpha solenoid" for a ...
"Regulation of the nuclear gene that encodes the alpha-subunit of the mitochondrial F0F1-ATP synthase complex. Activation by ... "Novel consensus DNA-binding sequence for BRCA1 protein complexes". Molecular Carcinogenesis. 38 (2): 85-96. doi:10.1002/mc. ... Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (Apr 1996). "A "double adaptor" method for improved shotgun library ... Breen GA, Jordan EM (Aug 1999). "Transcriptional activation of the F(1)F(0) ATP synthase alpha-subunit initiator element by ...
Adaptor-related protein complex 2 (AP-2 complexes) functions during receptor-mediated endocytosis to trigger clathrin assembly ... The protein interacts with and phosphorylates a subunit of the AP-2 complex, which promotes binding of AP-2 to sorting signals ... "Dual engagement regulation of protein interactions with the AP-2 adaptor alpha appendage". The Journal of Biological Chemistry ... Adaptor-associated protein kinase 1 also known as AP2-associated protein kinase 1 is an enzyme that in humans is encoded by the ...
The DDB1 adaptor protein was initially characterized as the large subunit of a heterodimeric complex (UV-DDB) that was found to ... CUL4A protein is 759 amino acids long and forms an extended, rigid structure primarily consisting of alpha-helices. At the N- ... DDB2 is a DCAF protein and is both a ubiquitination substrate of the CRL4 complex and also serves as an E3 ligase protein for ... The smaller subunit of this Damaged DNA Binding protein complex is known as DDB2 and is able to directly bind DNA lesions ...
... consists of seven subunits which compose the heteroheptameric protein complex. The primary function of adaptors is the ... is made ARF binds to the cytosolic side of the cis-Golgi membrane and inserts the myristoylated N-terminal amphipathic alpha- ... COPI is a coatomer, a protein complex that coats vesicles transporting proteins from the cis end of the Golgi complex back to ... The order in which adaptor proteins associate with cargo, or adaptor proteins associate with ARFs is unclear, however, in order ...
"Entrez Gene: AP2A2 adaptor-related protein complex 2, alpha 2 subunit". Chen H, Fre S, Slepnev VI, Capua MR, Takei K, Butler MH ... AP-2 complex subunit alpha-2 is a protein that in humans is encoded by the AP2A2 gene. AP2A2 has been shown to interact with ... Robinson MS (Mar 1989). "Cloning of cDNAs encoding two related 100-kD coated vesicle proteins (alpha-adaptins)". The Journal of ... the cytoplasmic domains of human and simian retroviral transmembrane proteins with components of the clathrin adaptor complexes ...
adaptor related protein complex 1 subunit sigma 2. acts_upstream_of_or_within. ISO. (PMID:20203623). MGI. PMID:20203623. NCBI ... G protein subunit alpha transducin 1. acts_upstream_of_or_within. ISO. (PMID:20844144). MGI. PMID:20844144. NCBI chr20: ... G protein subunit alpha transducin 2. involved_in. acts_upstream_of_or_within. IEA. ISO. (PMID:20844144), (PMID:30225342). ... PILR alpha associated neural protein. acts_upstream_of_or_within. ISO. (PMID:31511635). MGI. PMID:31511635. NCBI chr27: ...
The IKK core complex seems to associate with regulatory or adapter proteins to form a IKK-signalosome holo-complex. The IKK ... probably four alpha/CHUK-beta/IKBKB dimers are associated with four gamma/IKBKG subunits. ... I-kappa-B kinase subunit gamma; IkB kinase gamma subunit; IkB kinase subunit gamma; IkB kinase-associated protein 1; Ikbkg; IKK ... IkB kinase associated protein 1; IkB kinase subunit gamma; Inhibitor of nuclear factor kappa B kinase subunit gamma; AMCBX1; ...
Protein IKBKB , Inhibitor of nuclear factor kappa-B kinase subunit beta - Also known as IKKB_HUMAN, IKBKB, IKKB. Serine kinase ... The IKK core complex seems to associate with regulatory or adapter proteins to form a IKK-signalosome holo-complex (PubMed: ... core complex consisting of CHUK, IKBKB and IKBKG; probably four alpha/CHUK-beta/IKBKB dimers are associated with four gamma/ ... acts as an adapter protein for NFKBIA degradation in UV-induced NF-kappa-B activation (PubMed:11297557). Phosphorylates RIPK1 ...
... protein that we name clathrin interacting protein localized in the trans-Golgi region (Clint). It localizes predominantly to ... Adaptor Protein Complex gamma Subunits * Adaptor Proteins, Vesicular Transport * CLINT1 protein, human ... with the appendage domain of beta2-adaptin and to a lesser extent with the appendage domain of alpha-adaptin. Moreover, the ... protein that we name clathrin interacting protein localized in the trans-Golgi region (Clint). It localizes predominantly to ...
... adaptor related protein complex 1 sigma 2 subunit (AP1S2), PHD finger protein 21A (PHF21A), lipoma preferred partner (LPP), and ... transcription factor AP-2 alpha (TFAP2A) showed similar expression patterns in OA FLS and OA synovial tissue datasets in Gene ... Kidney is a highly complex organ and the pathogenesis underlying kidney organization involves complex cell-to-cell interaction ... Exosomal protein from PTECs treated with high glucose (HG) was purified and examined using liquid chromatography-tandem mass ...
BCKDHA: branched chain keto acid dehydrogenase E1 subunit alpha. *BCKDHB: branched chain keto acid dehydrogenase E1 subunit ... BMPR1A: bone morphogenetic protein receptor type 1A. *BMPR2: bone morphogenetic protein receptor type 2 ... BCS1L: BCS1 homolog, ubiquinol-cytochrome c reductase complex chaperone. *BDNF: brain derived neurotrophic factor ... BICD2: BICD cargo adaptor 2. *BIN1: bridging integrator 1. *BLM: BLM RecQ like helicase ...
Protein function: Receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule fadd recruits ... Various tradd-interacting proteins such as trafs, rip and possibly fadd, are recruited to the complex by their association with ... Subunit: Binding of TNF to the extracellular domain leads to homotrimerization. The aggregated death domains provide a novel ... Type I membrane protein and secreted.. Post-translational modification: The soluble form is produced from the membrane form by ...
Actin-binding proteins (ABPs), by interacting with actin, regulate the polymerization, depolymerization, bundling, and cross- ... The F-actin-binding protein switch-associated protein 70 (SWAP70, SWAP switch B cell complex 70 kDa subunit) is involved in the ... J. M. Baisden, Y. Qian, H. M. Zot, and D. C. Flynn, "The actin filament-associated protein AFAP-110 is an adaptor protein that ... an ABP capping actin protein, muscle Z-line alpha subunit 1 (CAPZA1), is overexpressed in gastric epithelial cells infected ...
AP1S2 encodes an adaptin protein that constitutes part of the adaptor protein complex found at the cytoplasmic face of coated ... Aberrant endocytic processing through disruption of adaptor protein complexes is likely to result from the AP1S2 mutations ... AP1S2 is the first reported XLMR gene that encodes a protein directly involved in the assembly of endocytic vesicles. ... The complex mediates the recruitment of clathrin to the vesicle membrane. ...
adaptor-related protein complex 2, beta 1 subunit 1.53327 PTPN11 protein tyrosine phosphatase, non-receptor type 11 1.51775 ... ankyrin repeat and sterile alpha motif domain containing 1B 0.492728 ZNF583 zinc finger protein 583 0.487744 ... about genes and proteins. Database (Oxford). 2016 Jul 3;2016. pii: baw100. ...
TRAPPC2: trafficking protein particle complex subunit 2. *TREM2: triggering receptor expressed on myeloid cells 2 ... TFAP2A: transcription factor AP-2 alpha. *TFAP2B: transcription factor AP-2 beta ... TCIRG1: T cell immune regulator 1, ATPase H+ transporting V0 subunit a3 ... TYROBP: transmembrane immune signaling adaptor TYROBP. *TYRP1: tyrosinase related protein 1. *About MedlinePlus ...
adaptor-related protein complex 1, sigma 1 subunit. Molecular. brain. Human. AP1S1. 12.0% Decrease Gene Expression Level. Add. ... actin, alpha 1, skeletal muscle. Molecular. brain. Human. ACTA1. 16.0% Decrease Gene Expression Level. Add. ...
Transcription factors enriched in NAC and Myb protein domains would target preferentially the genes encoding proteins more ... 1663 proteins could be used for comparison with datasets assessed using transcriptomic approaches and for quantitative protein ... Many proteins likely involved in cell wall and sugar metabolism, aroma and color, change their abundance during the transition ... Close to 26% of the genes that code for the proteins assessed displayed higher expression at ripe fruit compared to other fruit ...
Structure of hemolysin A secretion system HlyB/D complex ... Alpha-hemolysin translocation ATP-binding protein HlyB. A [auth ... Three membrane proteins-an inner membrane ABC transporter HlyB, an adaptor protein HlyD, and an outer membrane porin TolC-are ... reveal that the inner membrane complex is a hetero-dodecameric assembly comprising three HlyB homodimers and six HlyD subunits ... Membrane fusion protein (MFP) family protein,Hemolysin secretion protein D, chromosomal. G [auth H]. H [auth L]. I [auth D]. J ...
Two Clathrin Adaptor Protein Complexes Instruct Axon-Dendrite Polarity.. Li P, Merrill SA, Jorgensen EM, Shen K. Neuron 2016 ... All these motifs are believed to bind to the sigma subunit of activated adaptin complexes (AP-1, AP-2 and AP-3). These clathrin ... The gamma/sigma1 and alpha/sigma2 hemicomplexes of clathrin adaptors AP-1 and AP-2 harbor the dileucine recognition site.. ... Structural basis of HIV-1 Vpu-mediated BST2 antagonism via hijacking of the clathrin adaptor protein complex 1.. Jia X, Weber E ...
GNAO1; G protein subunit alpha o1 [KO:K04534]. 2778 GNAS; GNAS complex locus [KO:K04632]. ... MYD88; MYD88 innate immune signal transduction adaptor [KO:K04729]. 3654 IRAK1; interleukin 1 receptor associated kinase 1 [KO: ... protein phosphatase 2 catalytic subunit alpha [KO:K04382] [EC:3.1.3.16]. 5516 PPP2CB; protein phosphatase 2 catalytic subunit ... CD3D; CD3 delta subunit of T-cell receptor complex [KO:K06450]. 916 CD3E; CD3 epsilon subunit of T-cell receptor complex [KO: ...
Hermansky-Pudlak syndrome protein complexes interface with phosphatidylinositol 4-kinase type II-alpha (PI4KII-alpha) in ... Hermansky-Pudlak syndrome-associated genes participate in at least 4 distinct protein complexes: the adaptor complex AP-3; BLOC ... HPS-2 is caused by a mutation in the gene encoding the beta-3A subunit of the heterotetrameric AP3 complex (AP3BA), which ... impact PI4KII-alpha inclusion into AP-3 complexes. BLOC-1, PI4KII-alpha, and AP-3 belong to a tripartite complex involved with ...
... including IFN alpha, BIFN beta, IFN alpha receptor 1, and IFN gamma. ... Explore the JAK/STAT signaling pathway and find antibodies to detect some of its target proteins, ... A second adapter that facilitates JAK/STAT pathway activation is STATIP (STAT-Interacting Protein), a WD40 protein. STATIPs can ... interaction with the Elongin-B/C complex and couples the SOCS and associated target proteins JAKs to the proteasomal protein ...
adaptor related protein complex 1 su.... ARMCX3. 51566. ARMCX3. armadillo repeat containing X-linked.... ... ER membrane protein complex subunit .... C3AR1. 719. C3AR1. complement C3a receptor 1 [Source:HG.... ... NGFI-A binding protein 2 [Source:HGN.... NAPA. 8775. NAPA. NSF attachment protein alpha [Source.... ... trafficking protein particle complex.... TRAPPC2P1. 10597. TRAPPC2B. trafficking protein particle complex.... TRDN. 10345. TRDN ...
Hermansky-Pudlak syndrome protein complexes interface with phosphatidylinositol 4-kinase type II-alpha (PI4KII-alpha) in ... Hermansky-Pudlak syndrome-associated genes participate in at least 4 distinct protein complexes: the adaptor complex AP-3; BLOC ... HPS-2 is caused by a mutation in the gene encoding the beta-3A subunit of the heterotetrameric AP3 complex (AP3BA), which ... impact PI4KII-alpha inclusion into AP-3 complexes. BLOC-1, PI4KII-alpha, and AP-3 belong to a tripartite complex involved with ...
Keywords: گوانوزین تری فسفات; AKT (PKB); protein kinase B; AP2; adaptor protein 2; APPL1; adaptor protein containing PH domain ... 5â ²-AMP activated protein kinase; AMPKα (also AAK-2); AMPKα subunit; ATP; adenosine triphosphate; Bcl-2; B-cell lymphoma 2; ... Pyrrole N-H anion complexes Keywords: گوانوزین تری فسفات; ADP; adenosine diphosphate; AMP; adenosine monophosphate; ATP; ... Keywords: گوانوزین تری فسفات; Guanosine triphosphate; Peroxidase-like activity; Alkaline phosphatase; Alpha-fetoprotein; ELISA ...
GGA proteins regulate vesicular traffic between Golgi and endosomes and might work as antagonists for retromer complex mediated ... Mutation in the retromer-complex protein VPS35, which is involved in endosome to Golgi transport, was suggested to cause ... To investigate the role of the GGAs in the α-syn oligomerization and/or secretion process we utilized protein-fragment ... Several age-related neurodegenerative disorders are associated with protein misfolding and aggregation of toxic peptides. α- ...
Suppression of micro1 subunit of the adaptor protein complex 2 reduces dengue virus release. Virus Genes 2020, 56, 27-36. [ ... Inhibition of NF-kappaB nuclear translocation via HO-1 activation underlies alpha-tocopheryl succinate toxicity. J. Nutr. ... For the protein expressions, Western blot analysis was conducted with protein samples obtained from liver homogenates, and the ... For the protein expressions, Western blot analysis was conducted with protein samples obtained from liver homogenates, and the ...
NUF2, NDC80 kinetochore complex component. protein-coding. NR2F1. nuclear receptor subfamily 2 group F member 1. protein-coding ... N-acetylated alpha-linked acidic dipeptidase like 2. protein-coding. NEXMIF. neurite extension and migration factor. protein- ... NUMB, endocytic adaptor protein. protein-coding. NOL7. nucleolar protein 7. protein-coding. ... protein-coding. NIF3L1. NGG1 interacting factor 3 like 1. protein-coding. NDUFC2. NADH:ubiquinone oxidoreductase subunit C2. ...
pump into RNA-Induced Silencing Complex( RISC) and adaptor membrane. The active download جبر خطی is inferred to a free ... The residue follows N-terminal but complex of SLC16A1 inflammation does tissue subunits and iron direction in shift and ... flooding nucleotides that attract packaged to the protein and secreted to complex credits via the cytosolic death. These ... Since interleukin-1 of these receptors are required in the download جبر, cobalt and consultation, they are an oxidative alpha ...
... and protein level. In addition, an elevated level of tumor necrosis factor, alpha-induced protein 8-like 1 (Tipe1) exacerbates ... All mitophagy receptors and adapters form a complex network and can regulate each other.. PHARMACOLOGIC INTERVENTION IN ... DNA-dependent protein kinase, catalytic subunit (DNA-PKcs)/p53 pathway, and BDNF is positively regulated by BNIP3 [66] and ... BCL2 interacting protein 3; GFP-LC3, green fluorescent protein-light chain 3; mRFP-LC3, monomeric red fluorescent protein-light ...
TTP is phosphorylated extensively in cells and its mRNA destabilization activity is regulated by protein phosphorylation. ... ... family proteins contain conserved tandem CCCH zinc-finger binding to AU-rich elements and C-terminal NOT1-binding domain. ... The largest subunit of CCR4-NOT, namely CCR4-NOT1 complex subunit 1 (CNOT1), serves as a hub of protein-protein interactions [ ... p38-activated protein kinase 2 (MK2) at serines 52 and 178 in mouse macrophages to allow binding of 14-3-3 adaptor proteins, ...
  • disrupts IKBKB-IKBKG interaction preventing I-kappa-B-kinase (IKK) core complex formation and leading to a decrease of IKBKB phosphorylation and NF-kappaB activation (PubMed:27426725). (icr.ac.uk)
  • JAK belongs to a family of non-receptor protein tyrosine kinases of approximately 130 kDa, comprising of JAK1, JAK2, JAK3, and TYK2 (non-receptor Protein Tyrosine Kinase-2). (thermofisher.com)
  • In obesity and diabetes, two classical pathways appear to regulate mitophagy, including PTEN-induced putative kinase 1 (PINK1)/Parkin-dependent mitophagy and receptors/adapters-dependent mitophagy. (e-dmj.org)
  • We demonstrated that Ser316 was phosphorylated by p90 ribosomal S6 kinase 1 (RSK1) and p38-activated protein kinase (MK2), and dephosphorylated by Protein Phosphatase 2A (PP2A). (researchsquare.com)
  • TTP can be phosphorylated by mitogen-activated protein kinase (MAPK) p38-activated protein kinase 2 (MK2) at serines 52 and 178 in mouse macrophages to allow binding of 14-3-3 adaptor proteins, which inhibits the mRNA destabilizing activity of TTP [ 17 , 18 ]. (researchsquare.com)
  • The adapter molecule fadd recruits caspase-8 to the activated receptor. (lu.se)
  • Adaptin-binding acidic dileucine motifs and variants thereof occur almost exclusively on the cytosolic side of membrane proteins, mostly integral (transmembrane) proteins. (eu.org)
  • In the latter, they are frequently located near the protein N- or C-termini, with relative proximity (within 10-100aa) to a transmembrane segment. (eu.org)
  • Mutations in the gene encoding the Sigma 2 subunit of the adaptor protein 1 complex, AP1S2, cause X-linked mental retardation. (ox.ac.uk)
  • AP1S2 encodes an adaptin protein that constitutes part of the adaptor protein complex found at the cytoplasmic face of coated vesicles located at the Golgi complex. (ox.ac.uk)
  • Aberrant endocytic processing through disruption of adaptor protein complexes is likely to result from the AP1S2 mutations identified in the three XLMR-affected families, and such defects may plausibly cause abnormal synaptic development and function. (ox.ac.uk)
  • AP1S2 is the first reported XLMR gene that encodes a protein directly involved in the assembly of endocytic vesicles. (ox.ac.uk)
  • Receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. (lu.se)
  • Crystal structure of the soluble human 55 kd TNF receptor-human TNF complex: implications for TNF receptor activation. (lu.se)
  • STATs are latent cytoplasmic transcription factors that become activated after recruitment to an activated receptor complex. (thermofisher.com)
  • Intracellular activation occurs when ligand binding induces the multimerization of receptor subunits. (thermofisher.com)
  • For some ligands, such as Epo (erythropoietin) and GH (growth hormone), the receptor subunits are bound as homodimers while for others, such as Ifns (interferons) and ILs (interleukins), the receptor subunits are heteromultimers. (thermofisher.com)
  • For signal propagation, the cytoplasmic domains of two receptor subunits must be associated with JAK tyrosine kinases. (thermofisher.com)
  • The phosphorylated STATs then dissociate from the receptor heterodimer and bind to IRF9/p48, a member of the IRF (Interferon Regulatory Factor-9) family, forming a trimeric major interferon gene factor known as ISGF3 (Interferon-Stimulated Transcription Factor-3) complex. (thermofisher.com)
  • G protein-coupled receptor class C g. (gsea-msigdb.org)
  • The receptor is the dinucleotide through the complex sodium- into the proliferation. (erik-mill.de)
  • Type I membrane protein and secreted. (lu.se)
  • The latter dileucine motifs were implicated in membrane protein sorting to vacuoles or tonoplasts. (eu.org)
  • probably four alpha/CHUK-beta/IKBKB dimers are associated with four gamma/IKBKG subunits. (icr.ac.uk)
  • Recombinantly expressed Clint interacts directly with the gamma-appendage domain of AP-1, with the clathrin N-terminal domain through the peptide motif (423)LFDLM, with the gamma-adaptin ear homology domain of Golgi-localizing, gamma-adaptin ear homology domain 2, with the appendage domain of beta2-adaptin and to a lesser extent with the appendage domain of alpha-adaptin. (nih.gov)
  • All these motifs are believed to bind to the sigma subunit of activated adaptin complexes (AP-1, AP-2 and AP-3). (eu.org)
  • Sigma subunits of AP complexes differ slightly in their surface charge densities and binding groove geometry, allowing for both generic and selective interactions with protein partners. (eu.org)
  • Due to the similarity of the adaptin sigma subunits, variant dileucine motifs may have overlapping specificities, being capable of binding multiple adaptins. (eu.org)
  • The impaired function of specific organelles indicates that the causative genes encode protein complexes that regulate vesicle trafficking in the endolysosomal system including AP-3, BLOC-1, BLOC-2, and BLOC-3. (medscape.com)
  • GGA proteins regulate vesicular traffic between Golgi and endosomes and might work as antagonists for retromer complex mediated transport. (aging-us.com)
  • Our results suggest that the TTP-mediated mRNA stability is modulated by Ser316 phosphorylation to regulate the TTP interaction with CCR4-NOT deadenylase complex. (researchsquare.com)
  • Several ARE-binding proteins have been shown to regulate mRNA turnover/decay [ 8 ], which is initiated by deadenylation via deadenylases including poly(A)-specific ribonuclease (PARN) and the polyA nuclease 2 (PAN2)-PAN3 and carbon catabolite repression (CCR4)-negative on TATA-less (NOT) complexes [ 9 ]. (researchsquare.com)
  • enzymes at the angiogenic download Conference of the Symbols, Units and Nomenclature (S. U. N.) Commission of the International Union of Pure can regulate the features( proteins or recognition) down their French glucose, at an either cardiac fibroblast( mainly to 108 cytosol). (familie-vos.de)
  • This initiates the activation of two Janus-family tyrosine kinases, JAK1 and TYK2, followed by phosphorylation of STAT1 and STAT2 (Signal Transducers and Activators of Transcription) proteins. (thermofisher.com)
  • HPS-2 is caused by a mutation in the gene encoding the beta-3A subunit of the heterotetrameric AP3 complex ( AP3BA ), which assists in the vesicle formation from the trans-Golgi network or late endosome. (medscape.com)
  • Mutation in the retromer-complex protein VPS35, which is involved in endosome to Golgi transport, was suggested to cause familial PD. (aging-us.com)
  • HPS-2 is caused by a mutation in the gene encoding the beta-3A subunit of the heterotetrameric AP3 complex (ADTB3A), which resides on chromosome 5. (medscape.com)
  • We have characterized a novel clathrin-binding 68-kDa epsin N-terminal homology domain (ENTH-domain) protein that we name clathrin interacting protein localized in the trans-Golgi region (Clint). (nih.gov)
  • Our results suggest that Clint might participate in the formation of clathrin-coated vesicles at the level of the trans-Golgi network and remains associated with the vesicles longer than clathrin and adaptors. (nih.gov)
  • Golgi proteins allow Also was been responses like the Golgins, initially publicly as zero polypeptides like the COG protein. (familie-vos.de)
  • Within the nucleus, acts as an adapter protein for NFKBIA degradation in UV-induced NF-kappa-B activation (PubMed:11297557). (icr.ac.uk)
  • A common feature of these age-related diseases is protein misfolding and aggregation of toxic peptides due to age-related decline of cellular functions including protein sorting and degradation mechanisms. (aging-us.com)
  • For forms that have AGO2, deficiency of the pathway complex of the viral CTD is degradation of the onset music. (erik-mill.de)
  • Specific mRNAs can be targeted by RNA-binding proteins to recruit deadenylase complexes for mRNA degradation [ 12 ]. (researchsquare.com)
  • Actin is an abundant and highly conserved protein that is mainly found in eukaryotic cells. (hindawi.com)
  • The IKK core complex seems to associate with regulatory or adapter proteins to form a IKK-signalosome holo-complex (PubMed:12612076). (icr.ac.uk)
  • The actin cytoskeleton, as the primary force-generating machinery in the cell, is a collection of F-actin with accessory and regulatory proteins [ 5 ]. (hindawi.com)
  • AP-2 complex subunit alpha-2 is a protein that in humans is encoded by the AP2A2 gene. (wikipedia.org)
  • Potential biomarkers for the ripening process, due to their differential accumulation and gene expression pattern, included a pectin methylesterase inhibitor, a gibbellerin 2-beta-dioxygenase, an omega-6 fatty acid desaturase, a homeobox-leucine zipper protein and an ACC oxidase. (biomedcentral.com)
  • The complex mediates the recruitment of clathrin to the vesicle membrane. (ox.ac.uk)
  • In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE (PubMed:11297557, PubMed:20410276). (icr.ac.uk)
  • They serve to initiate clathrin-mediated endocytosis or protein sorting and can work synergistically with the adaptin mu subunit binding YxxPhi-type motifs ( TRG_ENDOCYTIC_2 ). (eu.org)
  • Rouillard AD, Gundersen GW, Fernandez NF, Wang Z, Monteiro CD, McDermott MG, Ma'ayan A. The harmonizome: a collection of processed datasets gathered to serve and mine knowledge about genes and proteins . (maayanlab.cloud)
  • Close to 26% of the genes that code for the proteins assessed displayed higher expression at ripe fruit compared to other fruit developmental stages, based on published transcriptomic data. (biomedcentral.com)
  • Transcription factors enriched in NAC and Myb protein domains would target preferentially the genes encoding proteins more abundant in mature and ripe fruit, respectively. (biomedcentral.com)
  • Seven STAT proteins have been identified, STAT1 to 6, including STAT5a and STAT5b, which are encoded by distinct genes. (thermofisher.com)
  • This complex translocates to the nucleus and binds to the cis element ISRE (Ifn-stimulated Response Element), thereby initiating transcription of several Ifn-inducible genes. (thermofisher.com)
  • The impaired function of specific organelles indicates that the causative genes encode proteins operative in the formation of lysosomes and vesicles. (medscape.com)
  • The molecular server for tumor surface removal in the glutamate is with the subunit of guanyl-nucleotide to 7alpha-hydroxycholesterol. (erik-mill.de)
  • One molecular mechanism for TTP-mediated mRNA decay is recruitment of the CCR4-NOT deadenylase complex through direct interaction with CNOT1, resulting in decay of ARE-containing mRNAs [ 23 , 24 ]. (researchsquare.com)
  • Here, cryo-electron microscopy (cryo-EM) structures determined in two conformations reveal that the inner membrane complex is a hetero-dodecameric assembly comprising three HlyB homodimers and six HlyD subunits. (rcsb.org)
  • preservation precursor protein can ultimately refer with the return of an ER - additional or important. (erik-mill.de)
  • In the download جبر, the possible proteins of these two proteinases are in permeable regulators, flooding nucleotides that attract packaged to the protein and secreted to complex credits via the cytosolic death. (erik-mill.de)
  • Differential accumulation analysis between mature and ripe fruit revealed that 15% of the proteins identified were modulated by the ripening process, with glycogen and isocitrate metabolism, and protein localization overrepresented in mature fruit, as well as cell wall modification in ripe fruit. (biomedcentral.com)
  • In fungi and plants, dileucine motifs are often responsible for the vacuolar or tonoplast localization of proteins carrying these motifs. (eu.org)
  • unsaturated mitogens bind via their NACHT complexes, silencing immune membrane of RIP2 suggestions that regulates hypothesized to dimerize their K63-linked formation, causing bilayer of the similar pyruvate. (erik-mill.de)
  • Endocytosis and/or vesicular sorting signals for membrane proteins. (eu.org)
  • Many proteins likely involved in cell wall and sugar metabolism, aroma and color, change their abundance during the transition from mature to ripe fruit. (biomedcentral.com)
  • Considering that LAMTOR1 is a protein upstream of mTORC1/p70S6K and that macrophages are directly related to inflammation, here, we used LAMTOR1 macrophage-specific knockout (MKO) mice to clarify the role of macrophage LAMTOR1 in inflammation and metabolism. (frontiersin.org)
  • Three membrane proteins-an inner membrane ABC transporter HlyB, an adaptor protein HlyD, and an outer membrane porin TolC-are required for secretion. (rcsb.org)
  • Functional studies indicate that oligomerization of HlyB and HlyD is essential for protein secretion and that polypeptides translocate through a canonical ABC transporter pathway in HlyB. (rcsb.org)
  • KDM1 proteins react IL4, which both is Ser1177 in an Lipid Structure and proteins as a binding B defect transporter opsonin to be valuable heat( Nelms et al. (familie-vos.de)
  • the interaction disrupts the IKK complex formation (PubMed:17684021). (icr.ac.uk)
  • the interaction is further increased in a TNF-alpha-dependent manner (PubMed:23091055). (icr.ac.uk)
  • Kidney is a highly complex organ and the pathogenesis underlying kidney organization involves complex cell-to-cell interaction within the heterogeneous kidney milieu. (bvsalud.org)
  • Advanced single-cell RNA sequencing (scRNA-seq) could reveal the complex architecture and interaction with the microenvironment in early DKD. (bvsalud.org)
  • Phosphorylation-mimic mutant of S316D resulted in dissociation with CCR4-NOT deadenylase complex through weakening interaction with CNOT1. (researchsquare.com)
  • TTP family proteins are serine/threonine-rich, and they appear as multiple bands in SDS-PAGE, indicating that they are highly phosphorylated [ 15 , 16 ]. (researchsquare.com)
  • To investigate the role of the GGAs in the α-syn oligomerization and/or secretion process we utilized protein-fragment complementation assays (PCA). (aging-us.com)
  • Part of a ternary complex consisting of TANK, IKBKB and IKBKG (PubMed:12133833). (icr.ac.uk)
  • Several age-related neurodegenerative disorders are associated with protein misfolding and aggregation of toxic peptides. (aging-us.com)
  • Part of a 70-90 kDa complex at least consisting of CHUK/IKKA, IKBKB, NFKBIA, RELA, ELP1 and MAP3K14 (PubMed:9751059). (icr.ac.uk)
  • The IKK complex associates with TERF2IP/RAP1, leading to promote IKK-mediated phosphorylation of RELA/p65 (By similarity). (icr.ac.uk)
  • TTP is phosphorylated extensively in cells and its mRNA destabilization activity is regulated by protein phosphorylation. (researchsquare.com)
  • Forms an NGF-induced complex with IKBKB, PRKCI and TRAF6 (By similarity). (icr.ac.uk)
  • Phosphorylated STATs then enter the nucleus by a mechanism that is dependent on Importin Alpha-5 (also called nucleoprotein interactor 1) and the Ran nuclear import pathway. (thermofisher.com)
  • Depending on organism, cell type as well as the nature of the adaptin complex bound, they can target either to cell surface or to specific, internal membrane-bound organelles (endosomes, lysosomes, melanosomes, synaptic vesicles, etc. (eu.org)
  • AP2 is chiefly involved in endocytosis of cell surface proteins and their trafficking to early or late endosomes. (eu.org)
  • They have a range of adaptin complexes they can associate with (AP-1, AP-2 and/or AP-3). (eu.org)
  • The dynamics of actin cytoskeleton is regulated by actin-binding proteins (ABPs) which participate in nucleation, elongation, and disassembling according to the need of the cells and play an important role in various biological systems, including muscle contraction, cytokinesis, cellular motility, plasmid separation in prokaryotes, and maintenance of cells and their physical integrities [ 6 ]. (hindawi.com)
  • GRB2 associated binding protein 1 [S. (gsea-msigdb.org)
  • Tristetraprolin (TTP) family proteins contain conserved tandem CCCH zinc-finger binding to AU-rich elements and C-terminal NOT1-binding domain. (researchsquare.com)
  • Tristetraprolin (TTP) is an extensively studied ARE-binding protein. (researchsquare.com)
  • ABPs, a class of proteins that also serve as a bridge between the cell membrane and the nucleus, transmit signals within the cytoplasm from outside to inside and from inside to outside [ 7 ]. (hindawi.com)
  • Interacts with hcv core protein. (lu.se)
  • Type 1 secretion systems (T1SSs) are widespread in pathogenic Gram-negative bacteria, extruding protein substrates following synthesis of the entire polypeptide. (rcsb.org)
  • It may form adaptors in different cell, achondroplasia, knockout, was LC and program( Trowbridge & Gallo 2002). (familie-vos.de)
  • The Ifn-AlphaBetaR consists of two subunits, IfnAR1 and IfnAR2, which form a heterodimer upon Ifn stimulation. (thermofisher.com)
  • single-copy proteins separate human enzymes with IL4, promoting from the cleavage that they manifest a high blood pol. (familie-vos.de)
  • Antibodies bound to the blocking peptide no longer bind to the epitope on the target protein. (affbiotech.com)
  • HPS3 is a biogenesis of the lysosome-related organelles complex (BLOC)-2 component. (medscape.com)
  • Because the expression of the beta-3A subunit is normally ubiquitous, deficiency of the beta-3A subunit leads to a precise phenotype in cells with a large number of intracellular granules (eg, neutrophils, natural killer cells, cytotoxic T lymphocytes, platelets, melanocytes). (medscape.com)
  • The largest subunit of CCR4-NOT, namely CCR4-NOT1 complex subunit 1 (CNOT1), serves as a hub of protein-protein interactions [ 11 ]. (researchsquare.com)
  • Furthermore, Ser316 and serines 52 and 178 were independently contributed to CCR4-NOT complex recruitment in the immunoprecipitation assay using phosphor-mimic mutants. (researchsquare.com)