Adaptor Protein Complex Subunits
Adaptor Protein Complex 1
Adaptor Protein Complex 2
Adaptor Protein Complex 4
Adaptor Protein Complex delta Subunits
Adaptor Protein Complex mu Subunits
Adaptor Proteins, Vesicular Transport
Adaptor Protein Complex gamma Subunits
Adaptor Protein Complex beta Subunits
Adaptor Protein Complex alpha Subunits
Protein Subunits
Adaptor Proteins, Signal Transducing
Clathrin
Multiprotein Complexes
Protein Binding
Human Characteristics
Adaptor protein complexes as the key regulators of protein sorting in the post-Golgi network. (1/7)
Adaptor protein (AP) complexes are cytosolic heterotetramers that mediate the sorting of membrane proteins in the secretory and endocytic pathways. AP complexes are involved in the formation of clathrin-coated vesicles (CCVs) by recruiting the scaffold protein, clathrin. AP complexes also play a pivotal role in the cargo selection by recognizing the sorting signals within the cytoplasmic tail of integral membrane proteins. Six distinct AP complexes have been identified. AP-2 mediates endocytosis from the plasma membrane, while AP-1, AP-3 and AP-4 play a role in the endosomal/lysosomal sorting pathways. Moreover, tissue-specific sorting events such as the basolateral sorting in polarized epithelial cells and the biogenesis of specialized organelles including melanosomes and synaptic vesicles are also regulated by members of AP complexes. The application of a variety of methodologies have gradually revealed the physiological role of AP complexes. (+info)Crystal structure of the clathrin adaptor protein 1 core. (2/7)
The heterotetrameric adaptor proteins (AP complexes) link the outer lattice of clathrin-coated vesicles with membrane-anchored cargo molecules. We report the crystal structure of the core of the AP-1 complex, which functions in the trans-Golgi network (TGN). Packing of complexes in the crystal generates an exceptionally long (1,135-A) unit-cell axis, but the 6-fold noncrystallographic redundancy yields an excellent map at 4-A resolution. The AP-1 core comprises N-terminal fragments of the two large chains, beta1 and gamma, and the intact medium and small chains, micro1 and sigma1. Its molecular architecture closely resembles that of the core of AP-2, the plasma-membrane-specific adaptor, for which a structure has been determined. Both structures represent an "inactive" conformation with respect to binding of cargo with a tyrosine-based sorting signal. TGN localization of AP-1 depends on the small GTPase, Arf1, and the phosphoinositide, PI-4-P. We show that directed mutations of residues at a particular corner of the gamma chain prevent recruitment to the TGN in cells and diminish PI-4-P-dependent, but not Arf1-dependent, liposome binding in vitro. (+info)The ubiquitously expressed Csk adaptor protein Cbp is dispensable for embryogenesis and T-cell development and function. (3/7)
Regulation of Src family kinase (SFK) activity is indispensable for a functional immune system and embryogenesis. The activity of SFKs is inhibited by the presence of the carboxy-terminal Src kinase (Csk) at the cell membrane. Thus, recruitment of cytosolic Csk to the membrane-associated SFKs is crucial for its regulatory function. Previous studies utilizing in vitro and transgenic models suggested that the Csk-binding protein (Cbp), also known as phosphoprotein associated with glycosphingolipid microdomains (PAG), is the membrane adaptor for Csk. However, loss-of-function genetic evidence to support this notion was lacking. Herein, we demonstrate that the targeted disruption of the cbp gene in mice has no effect on embryogenesis, thymic development, or T-cell functions in vivo. Moreover, recruitment of Csk to the specialized membrane compartment of "lipid rafts" is not impaired by Cbp deficiency. Our results indicate that Cbp is dispensable for the recruitment of Csk to the membrane and that another Csk adaptor, yet to be discovered, compensates for the loss of Cbp. (+info)Tetanus toxin is internalized by a sequential clathrin-dependent mechanism initiated within lipid microdomains and independent of epsin1. (4/7)
Ligand-receptor complexes are internalized by a variety of endocytic mechanisms. Some are initiated within clathrin-coated membranes, whereas others involve lipid microdomains of the plasma membrane. In neurons, where alternative targeting to short- or long-range trafficking routes underpins the differential processing of synaptic vesicle components and neurotrophin receptors, the mechanism giving access to the axonal retrograde pathway remains unknown. To investigate this sorting process, we examined the internalization of a tetanus neurotoxin fragment (TeNT HC), which shares axonal carriers with neurotrophins and their receptors. Previous studies have shown that the TeNT HC receptor, which comprises polysialogangliosides, resides in lipid microdomains. We demonstrate that TeNT HC internalization also relies on a specialized clathrin-mediated pathway, which is independent of synaptic vesicle recycling. Moreover, unlike transferrin uptake, this AP-2-dependent process is independent of epsin1. These findings identify a pathway for TeNT, beginning with the binding to a lipid raft component (GD1b) and followed by dissociation from GD1b as the toxin internalizes via a clathrin-mediated mechanism using a specific subset of adaptor proteins. (+info)Long double-stranded RNA produces specific gene downregulation in Giardia lamblia. (5/7)
(+info)The fifth adaptor protein complex. (6/7)
(+info)Trans-Golgi network morphology and sorting is regulated by prolyl-oligopeptidase-like protein PREPL and the AP-1 complex subunit mu1A. (7/7)
(+info)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 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 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 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.
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.
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.
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.
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.
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.
List of adaptins
AP4M1
X-linked intellectual disability
PIK3R4
AP3S2
AP3B2
AP1M1
AP2B1
AP2M1
AP1B1
AP4B1
AP1G2
AP1S1
AP3D1
AP3S1
AP2A2
AP3B1
AP1M2
AP3M1
AP1S2
CCDC47
NKG2D
AP5M1
Chromatin remodeling
Synergin gamma
Sec61 alpha 1
EPN2
AP1G1
AP5S1
MTMR12
Chromosome 12 open reading frame 71
AP2A2, adaptor-related protein complex 2, alpha 2 subunit - Creative BioMart
List of adaptins - Wikipedia
1gyv.1 | SWISS-MODEL Template Library
Sol Genomics Network
MMRRC:039291-MU
SGN Unigene - Show All Stored BLAST Hits - Sol Genomics Network
Immune cell - TMSB10 - The Human Protein Atlas
synaptic vesicle budding from endosome - Ontology Report - Rat Genome Database
Molecules | Free Full-Text | Methods for Studying Endocytotic Pathways of Herpesvirus Encoded G Protein-Coupled Receptors
O-GlcNAcylation of STAT5 controls tyrosine phosphorylation and oncogenic transcription in STAT5-dependent malignancies |...
Molecular basis of hypohidrotic ectodermal dysplasia: an update | Journal of Applied Genetics
Profile | Biosciences | University of Exeter
Viruses | Free Full-Text | African Swine Fever Virus Ubiquitin-Conjugating Enzyme Is an Immunomodulator Targeting NF-κB...
Hypermagnesemia: Practice Essentials, Kidney Failure, Other Causes
The promoter regions of intellectual disability-associated genes are uniquely enriched in LTR sequences of the MER41 primate...
YRC Public Data Repository - Gene Ontology GO Protein Search Results
CMMR - Gene Detail
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Intracellular trafficking
Research in the Rothman Lab | Rothman Lab
Adaptor protein complex-4 (AP-4) deficiency causes a novel autosomal recessive cerebral palsy syndrome with microcephaly and...
Plus it
MeSH Browser
Molecular Characterization of the Dbf4/Drf1-Dependent Kinase (DDK) and the DNA Replication Checkpoint Mediator Claspin in...
The multi-subunit GID/CTLH E3 ubiquitin ligase promotes cell proliferation and targets the transcription factor Hbp1 for...
eDGAR: AP1S3 gene page
Juan S. Bonifacino, Ph.D. | Principal Investigators | NIH Intramural Research Program
Category 1 - SFARI Gene
Reactome | AP2A2(1-939) [cytosol]
Dual-strand tumor-suppressor microRNA-145 ( miR-145-5p and miR-145-3p ) coordinately targeted MTDH in lung squamous cell...
Vesicular transport4
- Our lab is working to elucidate the underlying mechanisms of vesicular transport within cells and the secretion of proteins and neurotransmitters. (yale.edu)
- Adaptor Proteins, Vesicular Transport" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (jefferson.edu)
- This graph shows the total number of publications written about "Adaptor Proteins, Vesicular Transport" by people in this website by year, and whether "Adaptor Proteins, Vesicular Transport" was a major or minor topic of these publications. (jefferson.edu)
- Below are the most recent publications written about "Adaptor Proteins, Vesicular Transport" by people in Profiles. (jefferson.edu)
Adaptin4
- There are several types of adaptin, each related to a different AP complex. (wikipedia.org)
- sigma-adaptin subunit of adaptor protein complex 3 (AP-3) status:Confirmed UniProt:Q8T874 protein_id. (yeastrc.org)
- A family of medium adaptin protein subunits of approximately 45 KDa in size. (nih.gov)
- Adaptor protein complex 3 (ap-3) is an heterotetramer composed of two large adaptins (delta/ap3d1 and beta3a/ap3b2 or beta3b/ap3b1), a medium adaptin (mu3a/ap3m1 or mu3b/ap3m2) and a small adaptin (sigma3a/ap3s1 or sigma3b/ap3s2). (lu.se)
Multi-subunit2
- Particularly in yeast, an organism where gluconeogenesis and glycolytic activity are intermittently coordinated, the multi-subunit GID E3 ligase complex specifically targets the surplus of gluconeogenic enzymes, including the conserved Fructose-1,6-bisphosphatase 1 (Fbp1), for proteasomal degradation. (elifesciences.org)
- The majority of adaptor proteins exist as multi-subunit complexes, however monomeric varieties have also been found. (jefferson.edu)
Lysosome-related organelles2
- Ap-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. (lu.se)
- HPS3 is a biogenesis of the lysosome-related organelles complex (BLOC)-2 component. (medscape.com)
Transmembrane3
- Clathrin and cargo molecules are assembled into clathrin-coated pits on the plasma membrane together with an adaptor complex called AP-2 that links clathrin with transmembrane receptors, concluding in the formation of mature clathrin-coated vesicles (CCVs). (wormbook.org)
- We investigate the molecular mechanisms by which transmembrane proteins (referred to as cargo) are sorted to different compartments of the endomembrane system in eukaryotic cells. (nih.gov)
- The ap complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. (lu.se)
Ankyrin repeat domain1
- Mechanistically, we found that Rab40c binds the protein phosphatase 6 (PP6) complex and ubiquitylates one of its subunits, ankyrin repeat domain 28 (ANKRD28), thus leading to its lysosomal degradation. (life-science-alliance.org)
Catalytic subunit1
- Another focus of this study, DDK, is composed of the catalytic subunit Cdc7 and one of two distinct adaptor proteins, Drf1 or Dbf4. (caltech.edu)
Kinase2
- Replication blockages activate the ATR kinase which, in turn, activates the downstream effector kinase Chk1 through the mediator protein, Claspin. (caltech.edu)
- We characterized Xenopus Claspin as a kinase substrate of DDK which forms a stable nuclear complex with Cdc7 and Drf1 under both arrested and unperturbed replication conditions. (caltech.edu)
Mediate4
- Clathrin adaptor proteins, also known as adaptins, are proteins that mediate the formation of vesicles for intracellular trafficking and secretion. (wikipedia.org)
- However, chromatin binding-deficient Claspin proteins can still mediate Chk1 activation in Claspin-depleted extracts, albeit with reduced efficiency. (caltech.edu)
- Work in our laboratory focuses on the molecular machineries that mediate these processes, including (1) sorting signals and adaptor proteins that select cargo proteins for packaging into the transport carriers, (2) microtubule motors that drive movement of the transport carriers and other organelles through the cytoplasm, and (3) tethering factors that promote fusion of the transport carriers to acceptor compartments. (nih.gov)
- Since the early 1990s, Dr. Bonifacino's group has conducted research on signals and adaptor proteins that mediate protein sorting to endosomes and lysosomes. (nih.gov)
Genes8
- Recent advances in understanding the molecular events underlying hypohidrotic ectodermal dysplasia (HED) caused by mutations of the genes encoding proteins of the tumor necrosis factor α (TNFα)-related signaling pathway have been presented. (springer.com)
- Novel data were reviewed and discussed on the structure and functions of the components of TNFα-related signaling pathway, the consequences of mutations of the genes encoding these proteins, and the prospect for further investigations, which might elucidate the origin of HED. (springer.com)
- Mutations of these genes are responsible for systemic tooth agenesis, in addition to the defects of other ectodermal structures, and this review is limited to description of the function of their protein products. (springer.com)
- Interestingly, ID-associated genes exhibit promoter-localized MER41 LTRs that harbor TF binding sites (TFBSs) for not only STAT1 but also other immune TFs such as, in particular, NFKB1 (Nuclear Factor Kappa B Subunit 1) and STAT3 (Signal Transducer And Activator Of Transcription 3). (biorxiv.org)
- Of note, functionally-relevant differences between humans and chimpanzees are observed regarding the 3 main components of this pathway: i) the protein sequences of immunes TFs binding MER41 LTRs, ii) the insertion sites of MER41 LTRs in the promoter regions of ID-associated genes and iii) the protein sequences of the targeted ID-associated genes. (biorxiv.org)
- Deletions of multiple GID subunits compromise cell proliferation, and this defect is accompanied by deregulation of critical cell cycle markers such as the retinoblastoma (Rb) tumor suppressor, phospho-Histone H3 and Cyclin A. We identify the negative regulator of pro-proliferative genes Hbp1 as a bonafide GID/CTLH proteolytic substrate. (elifesciences.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)
- The impaired function of specific organelles indicates that the causative genes encode proteins operative in the formation of lysosomes and vesicles. (medscape.com)
Intracellular2
- He rose through the ranks to his current position as Head of the Section on Intracellular Protein Trafficking, NICHD, NIH. (nih.gov)
- 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)
Receptors2
- Many receptors and their associated ligands cluster into clathrin-coated pits by association with clathrin adaptor proteins such as the four-subunit complex AP2. (wormbook.org)
- Trafficking of yolk and yolk receptors also depends critically upon the activities of the endocytic Rab proteins RAB-5 , RAB-7 , and RAB-11 , known modulators of endocytosis in all eukaryotes ( Grant and Hirsh, 1999 ). (wormbook.org)
Plasma membrane1
- Endocytosis is the vesicle-mediated process used by all cells to internalize extracellular macromolecules, plasma membrane lipids, and plasma membrane proteins ( Figure 1 ). (wormbook.org)
Assembly protein complex1
- clathrin assembly protein complex 1, me. (cornell.edu)
Serine1
- OGT transfers O-GlcNAc moieties from UDP-GlcNAc to serine and threonine residues of proteins and O-GlcNAcase (OGA) catalyzes the opposite reaction to remove O-GlcNAc. (nature.com)
Pathway4
- Also, other proteins which involved in the same pathway with AP2A2 were listed below. (creativebiomart.net)
- Within the last 10 years significant progress has been made in understanding the pathogenesis of HED and this is mainly due to the discovery of unknown proteins and the elucidation of their function in signal transduction via the TNFα-related pathway. (springer.com)
- Finally, a survey of the human proteome has allowed us to map a protein-protein network which links the identified immune/MER41/cognition pathway to FOXP2 (Forkhead Box P2), a key TF involved in the emergence of human speech. (biorxiv.org)
- The pathway maps illustrate protein interactions and regulation to provide a comprehensive picture of signaling and disease processes. (bio-rad.com)
Ligase complex5
- Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for efficient chromosome alignment and cytokinesis. (ucsc.edu)
- The BCR(KLHL21) E3 ubiquitin ligase complex regulates localization of the chromosomal passenger complex (CPC) from chromosomes to the spindle midzone in anaphase and mediates the ubiquitination of AURKB. (ucsc.edu)
- Ubiquitination of AURKB by BCR(KLHL21) E3 ubiquitin ligase complex may not lead to its degradation by the proteasome. (ucsc.edu)
- Component of the BCR(KLHL21) E3 ubiquitin ligase complex, at least composed of CUL3, KLHL21 and RBX1. (ucsc.edu)
- Rab40c is a SOCS box-containing protein which binds Cullin5 to form a ubiquitin E3 ligase complex (Rab40c/CRL5) to regulate protein ubiquitylation. (life-science-alliance.org)
Membranes1
- Approximately 30% of total plasma magnesium is protein-bound and approximately 70% is filterable through artificial membranes (15% complexed, 55% free Mg 2+ ions). (medscape.com)
Endosomes2
- In early endosomes some ligand-receptor complexes dissociate due to the reduced pH of the endosomal lumen. (wormbook.org)
- Subunit of non-clathrin- and clathrin-associated adaptor protein complex 3 that plays a role in protein sorting in the late-golgi/trans-golgi network (tgn) and/or endosomes. (lu.se)
Regulate2
- Wnt proteins regulate developmental processes, tissue regeneration and stem cell maintenance. (exeter.ac.uk)
- There are many proteins known and rapidly being discovered which closely regulate this vital process, but the muscle - if not always the brains - is in the SNAREs. (yale.edu)
Beta3
- Autosomal-Recessive Mutations in AP3B2, Adaptor-Related Protein Complex 3 Beta 2 Subunit, Cause an Early-Onset Epileptic Encephalopathy with Optic Atrophy. (bvsalud.org)
- 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)
- 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)
Deletion3
- Methods and results This report describes an autosomal recessive form of spastic tetraplegic cerebral palsy with profound intellectual disability, microcephaly, epilepsy and white matter loss in a consanguineous family resulting from a homozygous deletion involving AP4E1 , one of the four subunits of the adaptor protein complex-4 (AP-4), identified by chromosomal microarray analysis. (bmj.com)
- Less pronounced severity of immunodeficiency can be due to a novel 2 bp-deletion (c.3222_3223delTG) in the final exon of AP3B1 , causing a frameshift and thus a prolonged altered HPS2 protein. (medscape.com)
- The place of the deletion is at the very C-terminal's end, preventing a complete loss of the HPS2 protein. (medscape.com)
Compartment1
- Compartmental specificity is encoded to a remarkable degree in the functional partnering of SNARE proteins, a fact which is in no way inconsistent with the emerging contribution of upstream regulatory components (like rabGTPases and tethering complexes) to domain/compartment specificity. (yale.edu)
Interactions1
- AP2A2 has direct interactions with proteins and molecules. (creativebiomart.net)
Molecules4
- We selected proteins and molecules interacted with AP2A2 here. (creativebiomart.net)
- 15 The dynamic addition and removal of O-GlcNAc has been described for multiple cytoplasmic and nuclear proteins and it affects the function of various signaling molecules and transcription factors. (nature.com)
- We identified a novel way of spreading Wnt proteins in vertebrates: Wnt molecules are mobilized on specific cell protrusions known as cytonemes. (exeter.ac.uk)
- A class of proteins involved in the transport of molecules via TRANSPORT VESICLES. (jefferson.edu)
Membrane2
- Clathrin adaptors in turn bind to the clathrin lattice which is thought to provide the force required to deform the membrane into a curved bud. (wormbook.org)
- Recombinant cognate SNAREs introduced into artificial bilayers or expressed ectopically on the outside of cells ( "flipped SNAREs") spontaneously and efficiently result in membrane (or cell) fusion, demonstrating that the SNARE complex is not only necessary but is sufficient for fusion. (yale.edu)
Component4
- YP170-GFP, like endogenous yolk, is a cholesterol binding/transport protein related to human ApoB-100, the major protein component of serum low-density lipoprotein (LDL). (wormbook.org)
- Component of the coat surrounding the cytoplasmic face of coated vesicles located at the golgi complex. (lu.se)
- It functions as a structural component and is phosphorylated by RIBOSOMAL PROTEIN S6 KINASES, integrating signals for cell growth and proliferation, especially during embryonic development. (bvsalud.org)
- Hermansky-Pudlak syndrome type 5 (HPS-5) results from a deficiency of the HPS5 protein, a component of BLOC-2. (medscape.com)
Transcription1
- 18 Both enzymes, OGT and OGA as well as multiple O-GlcNAcylated proteins are enriched at sites of active transcription in human cells. (nature.com)
Elucidation2
- We apply knowledge gained from this research to the elucidation of protein trafficking diseases including neurodevelopmental disorders. (nih.gov)
- His group discovered new sorting signals and adaptor proteins, and applied this knowledge to the elucidation of the causes of various human diseases including the Hermansky-Pudlak syndrome type 2 and hereditary spastic paraplegias. (nih.gov)
Residues1
- Cytokine binding to the cell surface leads to phosphorylation of the receptor complex by receptor associated Janus kinases (JAKs) at tyrosine residues. (nature.com)
Belongs1
- Belongs to the adaptor complexes large subunit family. (lu.se)
Xenopus1
- Here, we show that Claspin associates with several core replication fork proteins in Xenopus egg extracts. (caltech.edu)