A family of small adaptin protein complex subunits of approximately 19 KDa in size.
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.
A protein which is a subunit of RNA polymerase. It effects initiation of specific RNA chains from DNA.
An adaptor protein complex primarily involved in the formation of clathrin-related endocytotic vesicles (ENDOSOMES) at the CELL MEMBRANE.
Enzymes that catalyze DNA template-directed extension of the 3'-end of an RNA strand one nucleotide at a time. They can initiate a chain de novo. In eukaryotes, three forms of the enzyme have been distinguished on the basis of sensitivity to alpha-amanitin, and the type of RNA synthesized. (From Enzyme Nomenclature, 1992).
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 family of large adaptin protein subunits of approximately 100 kDa in size. They have been primarily found as components of ADAPTOR PROTEIN COMPLEX 2.
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

Distinct and redundant functions of mu1 medium chains of the AP-1 clathrin-associated protein complex in the nematode Caenorhabditis elegans. (1/17)

In the nematode Caenorhabditis elegans, there exist two micro1 medium chains of the AP-1 clathrin-associated protein complex. Mutations of unc-101, the gene that encodes one of the micro1 chains, cause pleiotropic effects (). In this report, we identified and analyzed the second mu1 chain gene, apm-1. Unlike the mammalian homologs, the two medium chains are expressed ubiquitously throughout development. RNA interference (RNAi) experiments with apm-1 showed that apm-1 and unc-101 were redundant in embryogenesis and in vulval development. Consistent with this, a hybrid protein containing APM-1, when overexpressed, rescued the phenotype of an unc-101 mutant. However, single disruptions of apm-1 or unc-101 have distinct phenotypes, indicating that the two medium chains may have distinct functions. RNAi of any one of the small or large chains of AP-1 complex (sigma1, beta1, or gamma) showed a phenotype identical to that caused by the simultaneous disruption of unc-101 and apm-1, but not that by single disruption of either gene. This suggests that the two medium chains may share large and small chains in the AP-1 complexes. Thus, apm-1 and unc-101 encode two highly related micro1 chains that share redundant and distinct functions within AP-1 clathrin-associated protein complexes of the same tissue.  (+info)

Sigma 1- and mu 1-Adaptin homologues of Leishmania mexicana are required for parasite survival in the infected host. (2/17)

The sorting of membrane-bound proteins from the trans-Golgi network to lysosomal/endosomal compartments is achieved by preferential inclusion into clathrin-coated vesicles. Contained within the cytoplasmic domains of such proteins, specific sequence motifs have been identified (tyrosine-based and/or di-leucine-based) that are essential for targeting and are recognized by a family of heterotetrameric adaptor complexes, which then recruit clathrin. These cytosolic protein complexes, which have been found in a wide variety of higher eukaryotic organisms, are essential for the development of multicellular organisms. In trypanosomatids, the adaptin-mediated sorting of proteins is largely uncharacterized. In order to identify components of the adaptor-complex machinery, this study reports the cloning and characterization of sigma 1- and mu 1-adaptin gene homologues from the eukaryotic protozoan parasite, Leishmania mexicana. Generation of sigma 1- and mu 1-adaptin gene deletion mutants shows that these promastigote parasites are viable in culture, but are unable to establish infection of macrophages or mice, indicating that adaptin function is crucial for pathogenesis in these unicellular organisms.  (+info)

The AP-3 clathrin-associated complex is essential for embryonic and larval development in Caenorhabditis elegans. (3/17)

The adaptor protein (AP) complexes are involved in membrane transport of many proteins. There are 3 AP complexes in C. elegans unlike mammals that have four. To study the biological functions of the AP-3 complexes of C. elegans, we sought homologues of the mouse and human genes that encode subunits of the AP-3 complexes by screening C. elegans genomic and EST sequences. We identified single copies of homologues of the m3, s3, b3 and d genes. The medium chain of AP-3 is encoded by a single gene in C. elegans but two different genes in mammals. Since there are no known mutations in these genes in C. elegans, we performed RNAi to assess their functions in development. RNAi of each of the genes caused embryonic and larval lethal phenotypes. APM-3 is expressed in most cells, particularly strongly in spermatheca and vulva. We conclude that the products of the C. elegans m3, s3, b3 and d genes are essential for embryogenesis and larval development.  (+info)

Mutations in the gene encoding the Sigma 2 subunit of the adaptor protein 1 complex, AP1S2, cause X-linked mental retardation. (4/17)

In a systematic sequencing screen of the coding exons of the X chromosome in 250 families with X-linked mental retardation (XLMR), we identified two nonsense mutations and one consensus splice-site mutation in the AP1S2 gene on Xp22 in three families. Affected individuals in these families showed mild-to-profound mental retardation. Other features included hypotonia early in life and delay in walking. 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. The complex mediates the recruitment of clathrin to the vesicle membrane. 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. AP1S2 is the first reported XLMR gene that encodes a protein directly involved in the assembly of endocytic vesicles.  (+info)

Mutations in the AP1S2 gene encoding the sigma 2 subunit of the adaptor protein 1 complex are associated with syndromic X-linked mental retardation with hydrocephalus and calcifications in basal ganglia. (5/17)

Fried syndrome, first described in 1972, is a rare X-linked mental retardation that has been mapped by linkage to Xp22. Clinical characteristics include mental retardation, mild facial dysmorphism, calcifications of basal ganglia and hydrocephalus. A large four-generation family in which the affected males have striking clinical features of Fried syndrome were investigated for linkage to X-chromosome markers; the results showed that the gene for this condition lies within the interval DXS7109-DXS7593 in Xp22.2. In total, 60 candidate genes located in this region, including AP1S2, which was recently shown to be involved in mental retardation, were screened for mutations. A mutation in the third intron of AP1S2 was found in all affected male subjects in this large French family. The mutation resulted in skipping of exon 3, predicting a protein with three novel amino-acids and with termination at codon 64. In addition, the first known large Scottish family affected by Fried syndrome was reinvestigated, and a new nonsense mutation, p.Gln66X, was found in exon 3. Using CT, both affected patients from the French family who were analysed had marked calcifications of the basal ganglia, as previously observed in the first Scottish family, suggesting that the presence of distinctive basal ganglia calcification is an essential parameter to recognise this syndromic disorder. It may be possible to use this feature to identify families with X-linked mental retardation that should be screened for mutations in AP1S2.  (+info)

Disruption of AP1S1, causing a novel neurocutaneous syndrome, perturbs development of the skin and spinal cord. (6/17)

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AP17 and AP19, the mammalian small chains of the clathrin-associated protein complexes show homology to Yap17p, their putative homolog in yeast. (7/17)

AP17 and AP19 are the smallest polypeptide chain components of AP-2 and AP-1, the clathrin-associated protein complexes found in coated structures of the plasma membrane and Golgi apparatus of mammalian cells. cDNA clones representing the entire coding sequence of AP17 and AP19 were isolated from rat and mouse brain cDNA libraries, respectively. Determination of their nucleotide sequence predicts proteins of 142 and 158 amino acids with Mr 17,018 and 18,733. A sequence comparison of rat brain AP17 with mouse brain AP19 demonstrates that the small chains are highly related. A computer search for other related proteins has uncovered in yeast a previously unknown gene whose DNA sequence encodes a protein homologous to the small chain of AP complexes. The yeast sequence predicts Yap17p, a protein with 147 amino acids and a Mr of 17,373 that is slightly more related to the mammalian AP17 chain than to its AP19 counterpart.  (+info)

Local clustering of transferrin receptors promotes clathrin-coated pit initiation. (8/17)

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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.

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.

A sigma factor is a type of protein in bacteria that plays an essential role in the initiation of transcription, which is the first step of gene expression. Sigma factors recognize and bind to specific sequences on DNA, known as promoters, enabling the attachment of RNA polymerase, the enzyme responsible for synthesizing RNA.

In bacteria, RNA polymerase is made up of several subunits, including a core enzyme and a sigma factor. The sigma factor confers specificity to the RNA polymerase by recognizing and binding to the promoter region of the DNA, allowing transcription to begin. Once transcription starts, the sigma factor is released from the RNA polymerase, which then continues to synthesize RNA until it reaches the end of the gene.

Bacteria have multiple sigma factors that allow them to respond to different environmental conditions and stresses by regulating the expression of specific sets of genes. For example, some sigma factors are involved in the regulation of genes required for growth and metabolism under normal conditions, while others are involved in the response to heat shock, starvation, or other stressors.

Overall, sigma factors play a crucial role in regulating gene expression in bacteria, allowing them to adapt to changing environmental conditions and maintain cellular homeostasis.

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.

DNA-directed RNA polymerases are enzymes that synthesize RNA molecules using a DNA template in a process called transcription. These enzymes read the sequence of nucleotides in a DNA molecule and use it as a blueprint to construct a complementary RNA strand.

The RNA polymerase moves along the DNA template, adding ribonucleotides one by one to the growing RNA chain. The synthesis is directional, starting at the promoter region of the DNA and moving towards the terminator region.

In bacteria, there is a single type of RNA polymerase that is responsible for transcribing all types of RNA (mRNA, tRNA, and rRNA). In eukaryotic cells, however, there are three different types of RNA polymerases: RNA polymerase I, II, and III. Each type is responsible for transcribing specific types of RNA.

RNA polymerases play a crucial role in gene expression, as they link the genetic information encoded in DNA to the production of functional proteins. Inhibition or mutation of these enzymes can have significant consequences for cellular function and survival.

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 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 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.

AP1S2: AP-1 complex subunit sigma-2. Adaptor protein complex 1 is found on the cytoplasmic face of vesicles located at 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 ... This nucleolar protein is involved in the processing and modification of tRNA. GDI1: RabGDI alpha makes a complex with ...
"Entrez Gene: AP3S2 adaptor-related protein complex 3, sigma 2 subunit". Dell'Angelica, E C; Ooi C E; Bonifacino J S (Jun 1997 ... AP-3 complex subunit sigma-2 is a protein that in humans is encoded by the AP3S2 gene. AP3S2 has been shown to interact with ... Dell'Angelica EC, Ohno H, Ooi CE, Rabinovich E, Roche KW, Bonifacino JS (Apr 1997). "AP-3: an adaptor-like protein complex with ... Dell'Angelica EC, Ooi CE, Bonifacino JS (1997). "Beta3A-adaptin, a subunit of the adaptor-like complex AP-3". J. Biol. Chem. ...
"Entrez Gene: AP1S1 adaptor-related protein complex 1, sigma 1 subunit". Montpetit A, Côté S, Brustein E, Drouin CA, Lapointe L ... AP-1 complex subunit sigma-1A is a protein that in humans is encoded by the AP1S1 gene. The protein encoded by this gene is ... Boehm M, Aguilar RC, Bonifacino JS (Nov 2001). "Functional and physical interactions of the adaptor protein complex AP-4 with ... Page LJ, Robinson MS (Nov 1995). "Targeting signals and subunit interactions in coated vesicle adaptor complexes". The Journal ...
"Entrez Gene: AP3S1 adaptor-related protein complex 3, sigma 1 subunit". Human AP3S1 genome location and AP3S1 gene details page ... AP-3 complex subunit sigma-1 is a protein that in humans is encoded by the AP3S1 gene. GRCh38: Ensembl release 89: ... "Interaction of insulin receptor substrate-1 with the sigma3A subunit of the adaptor protein complex-3 in cultured adipocytes". ... Dell'Angelica EC, Ohno H, Ooi CE, Rabinovich E, Roche KW, Bonifacino JS (March 1997). "AP-3: an adaptor-like protein complex ...
AP-1 complex subunit sigma-2 is a protein that in humans is encoded by the AP1S2 gene. Adaptor protein complex 1 is found at ... "Entrez Gene: AP1S2 adaptor-related protein complex 1, sigma 2 subunit". Huo L, Teng Z, Wang H, Liu X (March 2019). "A novel ... December 2006). "Mutations in the gene encoding the Sigma 2 subunit of the adaptor protein 1 complex, AP1S2, cause X-linked ... The protein encoded by this gene serves as the small subunit of this complex and is a member of the adaptin protein family. ...
AP complexes are heterotetramers composed of two large subunits (adaptins), a medium subunit (mu) and a small subunit (sigma). ... 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- ... The two major types of clathrin adaptor complexes are the heterotetrameric vesicular transport adaptor proteins (AP1-5), and ...
This gene encodes the alpha 1 adaptin subunit of the adaptor protein 2 (AP2 adaptors) complex found in clathrin coated vesicles ... sigma). The complex is part of the protein coat on the cytoplasmic face of coated vesicles which links clathrin to receptors in ... "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: ...
"Entrez Gene: AP2S1 adaptor-related protein complex 2, sigma 1 subunit". Pearse BM, Smith CJ, Owen DJ (2000). "Clathrin coat ... AP-2 complex subunit sigma is a protein that in humans is encoded by the AP2S1 gene. One of two major clathrin-associated ... Page LJ, Robinson MS (1995). "Targeting signals and subunit interactions in coated vesicle adaptor complexes". J. Cell Biol. ... "A novel spliced transcript of human CLAPS2 encoding a protein alternative to clathrin adaptor protein AP17". Gene. 220 (1-2): ...
Adaptins are clustered subunits of adaptor protein (AP) complexes. There are several types of adaptin, each related to a ... sigma): complex 1 AP1B1 AP1G1 AP1G2 AP1M1 AP1M2 AP1S1 AP1S2 AP1S3 complex 2 AP2A1 AP2A2 AP2B1 AP2M1 AP2S1 complex 3 AP3B1 AP3B2 ... 2011). "The Fifth Adaptor Protein Complex". PLOS Biology. 9 (10): e1001170. doi:10.1371/journal.pbio.1001170. PMC 3191125. PMID ... Clathrin adaptor proteins, also known as adaptins, are proteins that mediate the formation of vesicles for intracellular ...
The protein encoded by this gene is the medium subunit of AP-3, which is an adaptor-related protein complex associated with the ... a medium subunit (mu3), and a small subunit (sigma 3). Mutations in one of the large subunits of AP-3 have been associated with ... "Entrez Gene: AP3M1 adaptor-related protein complex 3, mu 1 subunit". Human AP3M1 genome location and AP3M1 gene details page in ... 2000). "Interactions of HIV-1 nef with the mu subunits of adaptor protein complexes 1, 2, and 3: role of the dileucine-based ...
AP (adaptor protein) complexes are found in coated vesicles and clathrin-coated pits. AP complexes connect cargo proteins and ... AP complexes are heterotetramers composed of two large subunits (adaptins), a medium subunit (mu) and a small subunit (sigma). ... 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- ...
AP-4 complex subunit beta-1 is a protein that in humans is encoded by the AP4B1 gene. The heterotetrameric adaptor protein (AP ... sigma-4 (AP4S1) AP4B1 has been shown to interact with AP4M1. AP4-complex-mediated trafficking plays a crucial role in brain ... "Entrez Gene: AP4B1 adaptor-related protein complex 4, beta 1 subunit". Hirst J, Bright NA, Rous B, Robinson MS (August 1999). " ... 2001). "Similar subunit interactions contribute to assembly of clathrin adaptor complexes and COPI complex: analysis using ...
AP-4 complex subunit sigma-1 is a protein that in humans is encoded by the AP4S1 gene. The heterotetrameric adaptor protein (AP ... "Entrez Gene: adaptor-related protein complex 4". Abou Jamra R, Philippe O, Raas-Rothschild A, Eck SH, Graf E, Buchert R, Borck ... Hirst J, Bright NA, Rous B, Robinson MS (1999). "Characterization of a fourth adaptor-related protein complex". Mol. Biol. Cell ... Dell'Angelica EC, Mullins C, Bonifacino JS (1999). "AP-4, a novel protein complex related to clathrin adaptors". J. Biol. Chem ...
AP-4 complex subunit epsilon-1 is a protein that in humans is encoded by the AP4E1 gene. The heterotetrameric adaptor protein ( ... sigma-4 (AP4S1). It is currently hypothesized that AP4-complex-mediated trafficking plays a crucial role in brain development ... 2001). "Similar subunit interactions contribute to assembly of clathrin adaptor complexes and COPI complex: analysis using ... "Entrez Gene: adaptor-related protein complex 4". Abou Jamra R, Philippe O, Raas-Rothschild A, Eck SH, Graf E, Buchert R, Borck ...
... and a small subunit σ (sigma ~20 kD), and named 1 through 5 corresponding to the 5 AP complexes. Components of COPI (cop one) a ... 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 ... but not closely related to the AP/TSET complexes. The individual proteins of the COPII complex are called SEC proteins, because ...
AP-5 complex subunit sigma (AP5S1) is a protein that in humans is encoded by the AP5S1 gene. The protein encoded by this gene ... In addition, damaging variants in the genes encoding two proteins that stably associate with the AP-5 adaptor complex are also ... Hirst, Jennifer; Irving, Carol; Borner, Georg H. H. (2012-11-21). "Adaptor protein complexes AP-4 and AP-5: new players in ... "The fifth adaptor protein complex". PLOS Biology. 9 (10): e1001170. doi:10.1371/journal.pbio.1001170. ISSN 1545-7885. PMC ...
The main complex of FA contains a nuclear multi-subunit complex of notably 8 FA proteins. This adds a single ubiquiting chain ... FANCE together with FANCC acts as the substrate adapter for this reaction Activated FANCD2 protein co-localizes with BRCA1 ( ... Sigma). It also then examines the use of micro satellite markers D6S422 and D6S1610, for linking. From this, a chromosomal ... This gene encodes the protein for complementation groufcrp E. A nuclear complex containing FANCE protein (as well as FANCC, ...
... adaptor protein complex mu subunits MeSH D12.776.543.990.150.500.750 - adaptor protein complex sigma subunits MeSH D12.776. ... adaptor protein complex alpha subunits MeSH D12.776.543.990.150.500.200 - adaptor protein complex beta subunits MeSH D12.776. ... adaptor protein complex delta subunits MeSH D12.776.543.990.150.500.400 - adaptor protein complex gamma subunits MeSH D12.776. ... adaptor protein complex 4 MeSH D12.776.543.990.150.500 - adaptor protein complex subunits MeSH D12.776.543.990.150.500.100 - ...
... ribosomal subunits, plasmids, DNA, RNA and proteins in fixed-angle rotors. Compared to microcentrifuges or high-speed ... to characterize the assembly and disassembly mechanisms of biomolecular complexes, to determine subunit stoichiometries, to ... Swinging-bucket rotors tend to be used very widely because of the huge flexibility of sample size through the use of adaptors. ... "Centrifugation Separations". Sigma-Aldrich. Retrieved 23 November 2020. Brakke, Myron K. (April 1951). "Density Gradient ...
2001). "Axonal transport of amyloid precursor protein is mediated by direct binding to the kinesin light chain subunit of ... and the Golgi complex. Thus, kinesin light chains function as adapter molecules and not motors per se. Although previously ... 2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer". Mol. Cell. Proteomics. 4 (6 ... Kinesin light chain 1 is a protein that in humans is encoded by the KLC1 gene. Conventional kinesin is a tetrameric molecule ...
... a Rho family GTPase-activating protein that interacts with signaling adapters Gab1 and Gab2". J. Biol. Chem. 278 (36): 34641-53 ... PX-RICS was found to be a necessary component for the export of this complex to the Golgi and then onwards to the cellular ... Benzinger A, Muster N, Koch HB, Yates JR, Hermeking H (2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector ... and weak binding to the NR2 subunits) suggests that there may be another pathway for it modifying spine structure as well. The ...
Moreover, cingulin forms a complex with JAM-A, a tight junction membrane protein. Most of cingulin protein interactions are ... Aijaz S, D'Atri F, Citi S, Balda MS, Matter K (May 2005). "Binding of GEF-H1 to the tight junction-associated adaptor cingulin ... Benzinger A, Muster N, Koch HB, Yates JR, Hermeking H (June 2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector ... each subunit containing a N-terminal globular "head" domain, a long α-helical coiled-coil "rod" domain and a small globular C- ...
AP1S2: AP-1 complex subunit sigma-2. Adaptor protein complex 1 is found on the cytoplasmic face of vesicles located at 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 ... This nucleolar protein is involved in the processing and modification of tRNA. GDI1: RabGDI alpha makes a complex with ...
Late endosomal/lysosomal adaptor, MAPK and MTOR activator 2. 0.8810. 29. AP2S1. Adaptor related protein complex 2 subunit sigma ... The Human Protein Atlas project is funded. by the Knut & Alice Wallenberg Foundation. ... DNA polymerase epsilon 4, accessory subunit. 0.9048. 29. GCNT2. Glucosaminyl (N-acetyl) transferase 2 (I blood group). 0.9048. ... General description of the gene and the encoded protein(s) using information from HGNC and Ensembl, as well as predictions made ...
adaptor related protein complex 1 subunit sigma 2. involved_in. ISO. (MGI:5617942,PMID:20203623). RGD. PMID:20203623. MGI: ... adaptor related protein complex 1 subunit gamma 1. involved_in. IDA. IMP. PMID:22539861. SynGO. PMID:22539861 PMID:22539861. ... adaptor related protein complex 3 subunit delta 1. involved_in. IDA. IBA. IMP. ISO. PMID:22539861. PMID:21873635. (MGI:6189637, ... Protein-Protein Interactions) PhenoMiner (Quatitative Phenotypes) Gene Annotator OLGA (Gene List Generator) AllianceMine ...
AP1S1 (Adaptor Related Protein Complex 1 Subunit Sigma 1): MEDNIK syndrome (Mental retardation, enteropathy, deafness, ... Black lines indicate protein-protein interactions. Green dashed lines indicate protein-DNA interactions between TFs and MER41 ... Black lines indicate protein-protein interactions. Dashed green lines indicate protein-DNA interactions between TFs and MER41 ... Protein interactors of these candidate targets were added in order to establish a final list of 80 proteins that are putatively ...
The experimental data is in the form of mass spectrometry, yeast two-hybrid, protein structure prediction, light microscopy and ... The YRC PDR provides for the searching of millions of protein descriptions from many databases to find proteins and public ... experimental data describing those proteins produced by the YRC. ... sigma-adaptin subunit of adaptor protein complex 3 (AP-3) ... Adaptor complexes medium subunit family status:Partially_confirmed UniProt:P90761 protein_id:CAB0279... MS ...
Gene Name: adaptor-related protein complex 2, sigma 1 subunit. MGI ID: MGI:2141861 ...
... adapter protein complex 1 subunit sigma 3 (AP1S3), TNFAIP3-interacting protein 1 (TNIP1), and the gene coding for alpha-1 ... IL-36 signaling involves a complex of IL-36 receptor (IL-36R) and IL-1R accessory protein (IL-1RAcP), disseminating ... and serum C-reactive protein levels (CRP), include fever higher than 38 °C and leukocytosis defined by a white blood cell (WBC ... a better understanding of the associated complex immunologic components is still needed. ...
Gene table of AP1S3 : adaptor related protein complex 1 sigma 3 subunit Gene-disease associations table Disease ID. Disease ... Nef-mediates down modulation of cell surface receptors by recruiting them to clathrin adapters. R-HSA-164938. 8.59. ... Nef mediated downregulation of MHC class I complex cell surface expression. R-HSA-164940. 9.66. ...
adaptor related protein complex 2 subunit sigma 1. 19. Rare Single Gene Mutation. 1. 3. ... SRP receptor subunit alpha. 11. Rare Single Gene Mutation. 1. 3. STXBP1. Syntaxin binding protein 1. 9. Rare Single Gene ... PHD finger protein 2. 9. Rare Single Gene Mutation. 1. 8. PHF21A. PHD finger protein 21A. 11. Rare Single Gene Mutation, ... KAT8 regulatory NSL complex subunit 1. 17. Rare Single Gene Mutation, Syndromic, Functional. 1. S. 11. ...
Adaptor protein complex, sigma subunit. Gene list. DPGLEAN05954. DPGLEAN14063. DPGLEAN14189. BGIBMGA009796. BGIBMGA000800. ...
adaptor-related protein complex 4, sigma 1 subunit HGNC id 575 *FLASH GENE ... adaptor complexes medium subunit family. CATEGORY adaptor , transport carrier SUBCELLULAR LOCALIZATION intracellular ... protein cell & other REGULATION ASSOCIATED DISORDERS. corresponding disease(s) SPG52 Susceptibility Variant & Polymorphism ... PROTEIN. PHYSICAL PROPERTIES STRUCTURE motifs/domains mono polymer heteromer , tetramer HOMOLOGY interspecies homolog to murine ...
adaptor related protein complex 4 sigma 1 subunit. 14q12. CV:PGCnp. GSMA_I. ... coatomer protein complex subunit zeta 2. 17q21.32. CV:PGCnp. DMG:Jaffe_2016. ... nitric oxide synthase 1 adaptor protein. 1q23.3. Association. CV:GWASdb. CV:PGCnp. Expression. GR_Ng. GSMA_IIA. PMID:cooccur. ... DnaJ heat shock protein family (Hsp40) member C6. 1p31.3. CV:PGCnp. DMG:Jaffe_2016. DNM:Fromer_2014. GSMA_IIA. RNA AND PROTEIN ...
adaptor-related protein complex 1, sigma 3 subunit Assay Type: SYBR® Green Assay Design: exonic Application: Gene Expression ... adaptor-related protein complex 1, sigma 3 subunit Assay Type: Probe Assay Design: exonic Application: Gene Expression Unique ... The pathway maps illustrate protein interactions and regulation to provide a comprehensive picture of signaling and disease ...
adaptor-related protein complex 2, sigma 1 subunit chr20_-_36107422 Show fit 0.39. ENSDART00000146055 ptchd4 Links *NCBI ... EARP complex and GARP complex interacting protein 1 chr20_+_23658791 Show fit 0.17. ENSDART00000192145 si:ch211-191d2.2 Links * ... RAB3 GTPase activating protein subunit 2 (non-catalytic) chr15_+_28116129 Show fit 0.37. ENSDART00000185157 unc119a Links *NCBI ... PTPRF interacting protein, binding protein 2b (liprin beta 2) chr21_-_38853737 Show fit 0.07. ENSDART00000184100 tlr22 Links * ...
adaptor-related protein complex 1, sigma 2 subunit. chr7_+_30291659 Show fit 2.30. ENSMUST00000014065.8 ENSMUST00000150892.1 ... G-protein beta/gamma-subunit complex binding(GO:0031683). 0.3. 2.3. GO:0051430. G-protein coupled serotonin receptor binding(GO ... cyclin-dependent protein kinase holoenzyme complex(GO:0000307). 0.2. 13.2. GO:0008023. transcription elongation factor complex( ... non-catalytic region of tyrosine kinase adaptor protein 2. chr13_+_44840686 Show fit 1.54. ENSMUST00000173906.1 Jarid2 Links * ...
adaptor-related protein complex 2, sigma 1 subunit. 7 232910 Mm.4514 E030003E18Rik RIKEN cDNA E030003E18 gene. 19 320092 ...
adaptor-related protein complex 2, sigma 1 subunit... [more]. Ap1s1. 1.272e-41. 43.97. adaptor protein complex AP-1, sigma 1 [ ... adaptor related protein complex 2 subunit sigma 1 ... [more]. ap1s1. 3.833e-41. 46.43. AP-1 complex subunit sigma-1A [Source: ... adaptor related protein complex 1 subunit sigma 1 ... [more]. zgc:162858. 2.006e-40. 46.43. AP-1 complex subunit sigma-2 [ ... adaptor related protein complex 2 subunit sigma 1 ... [more]. AP2S1. 2.744e-87. 88.65. adaptor related protein complex 2 ...
Gene Description : Adaptor related protein complex 1 subunit sigma 2. Molecular Function : ... Protein Class : Disease related genes, Human disease related genes, Predicted intracellular proteins. ...
... which encodes the adaptor-related protein complex 2 sigma (AP2σ) subunit, cause FHH type 3. These studies have demonstrated Gα, ... which encodes the G-protein α-11 (Gα,jats:sub,11,/jats:sub,) subunit, lead to FHH type 2 and ADH type 2, respectively; whilst ... is a family C G protein-coupled receptor, which detects alterations in Ca,jats:sup,2+,/jats:sup,,jats:sub,o,/jats:sub, ... which encodes the adaptor-related protein complex 2 sigma (AP2σ) subunit, cause FHH type 3. These studies have demonstrated Gα, ...
... and dileucine-based motifs of membrane-associated cargo proteins. Here we show that missense mutations of AP2 σ subunit (AP2S1 ... which internalizes plasma membrane constituents such as G protein-coupled receptors (GPCRs). AP2, a heterotetramer of α, β, μ ... affecting Arg15, which forms key contacts with dileucine-based motifs of CCV cargo proteins, result in familial hypocalciuric ... Adaptor protein-2 (AP2), a central component of clathrin-coated vesicles (CCVs), is pivotal in clathrin-mediated endocytosis, ...
... adaptor related protein complex 1 sigma 2 subunit (AP1S2), PHD finger protein 21A (PHF21A), lipoma preferred partner (LPP), and ... 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 ... The CRISPR systems usually require a guide RNA (gRNA) moiety to recruit and direct the nuclease complexes. In this respect, the ...
... adaptor protein complex 1 subunit sigma 3 (AP1S3), TNFAIP3-interacting protein 1 (TNIP1), and serpin family A member 3 (SERPINA ... Recognition Sigma-1 receptor antagonist 2 of pro-inflammatory cytokines such as tumor necrosis. ... Psoriatic arthritis (PsA) is definitely a complex inflammatory joint disease included in the spondyloarthropathy spectrum that ... Sigma-1 receptor antagonist 2 and swelling of bones, and it can progress to debilitating joint damage. Enthesitis and ...
Aps1, sigma subunit of the adaptin 1 complex [Ensembl].. 0.02. OrthoFinder. EOD24106. No alias. Adaptor protein 2 sigma subunit ... Adaptor protein 2 sigma subunit [Ensembl].. 0.02. OrthoFinder. EOD33031. No alias. Adaptor protein 2 sigma subunit [Ensembl].. ... proteasome core complex, alpha-subunit complex. IEP. Enrichment. BP. GO:0019941. modification-dependent protein catabolic ... AP complex, mu/sigma subunit [Interproscan].. 0.02. OrthoFinder. EOD06805. No alias. ...
Integrin-linked kinase (ILK) is a major structural adaptor protein governing signaling complex formation and cytoskeletal ... green fluorescent protein (GFP; Invitrogen), neurofilament-200 (NF-200; Sigma-Aldrich), cleaved caspase 3 (Asp175; Cell ... The β1 integrin subunit was shown previously to regulate OL process extension in vitro (Buttery and ffrench-Constant, 1999; ... One possibility is deactivation of the ILK-regulated neural Wiskott-Aldrich syndrome protein (N-WASP)/Arp2/3 complex (mediators ...
Experiments aimed at mapping UBCv1 inhibitory activity indicated that this viral protein acts upstream or at the level step of ... In this work, we have revealed that early viral protein UBCv1, the only known conjugating enzyme encoded by a virus, modulates ... In resting cells, IκB retains NF-κB complex subunits p65 and p50 in their inactive form in the cell cytosol. Thus, its ... Vaccinia Virus Protein C6 Is a Virulence Factor that Binds TBK-1 Adaptor Proteins and Inhibits Activation of IRF3 and IRF7. ...
zinc finger protein 280D -2.26557 AP4S1 adaptor-related protein complex 4, sigma 1 subunit -2.26459 ... protein phosphatase 5, catalytic subunit -1.85772 SDHC succinate dehydrogenase complex, subunit C, integral membrane protein, ... actin related protein 2/3 complex, subunit 3, 21kDa -1.55534 ATP5A1 ATP synthase, H+ transporting, mitochondrial F1 complex, ... protein phosphatase 1, regulatory subunit 3C 1.62181 GNAI2 guanine nucleotide binding protein (G protein), alpha inhibiting ...
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 ... Structural basis of HIV-1 Vpu-mediated BST2 antagonism via hijacking of the clathrin adaptor protein complex 1.. Jia X, Weber E ... These motifs bind directly to a highly conserved site located on the sigma subunits of adaptin complexes (adaptins AP1-4; Doray ...
  • Adaptor complexes medium subunit family status:Partially_confirmed UniProt:P90761 protein_id:CAB0279. (yeastrc.org)
  • Here we show that missense mutations of AP2 σ subunit (AP2S1) affecting Arg15, which forms key contacts with dileucine-based motifs of CCV cargo proteins, result in familial hypocalciuric hypercalcemia type 3 (FHH3), an extracellular calcium homeostasis disorder affecting the parathyroids, kidneys and bone. (ox.ac.uk)
  • The majority of adaptor proteins exist as multi-subunit complexes, however monomeric varieties have also been found. (lookformedical.com)
  • 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)
  • sigma-adaptin subunit of adaptor protein complex 3 (AP-3) status:Confirmed UniProt:Q8T874 protein_id. (yeastrc.org)
  • Aps1, sigma subunit of the adaptin 1 complex [Ensembl]. (ntu.edu.sg)
  • 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)
  • All these motifs are believed to bind to the sigma subunit of activated adaptin complexes (AP-1, AP-2 and AP-3). (eu.org)
  • One should avoid confusing the adaptin sigma-binding classical dileucine motifs discussed here, and the GGA-binding lysosomal targeting motifs (sometimes also called dileucine motifs). (eu.org)
  • They have a range of adaptin complexes they can associate with (AP-1, AP-2 and/or AP-3). (eu.org)
  • Adaptin-binding acidic dileucine motifs and variants thereof occur almost exclusively on the cytosolic side of membrane proteins, mostly integral (transmembrane) proteins. (eu.org)
  • 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)
  • Due to the similarity of the adaptin sigma subunits, variant dileucine motifs may have overlapping specificities, being capable of binding multiple adaptins. (eu.org)
  • A family of large adaptin protein subunits of approximately 100 kDa in size. (lookformedical.com)
  • A family of large adaptin protein complex subunits of approximately 90-130 kDa in size. (lookformedical.com)
  • A family of medium adaptin protein subunits of approximately 45 KDa in size. (lookformedical.com)
  • Vesicular transport proteins are distinguished from MEMBRANE TRANSPORT PROTEINS, which move molecules across membranes, by the mode in which the molecules are transported. (lookformedical.com)
  • Endocytosis and/or vesicular sorting signals for membrane proteins. (eu.org)
  • Adaptor protein 2 sigma subunit [Ensembl]. (ntu.edu.sg)
  • Finally, consistent with the differential expression of genes associated with proteasomal degradation in cln5 - cells, we also observed elevated amounts of a proteasome subunit and reduced proteasome 20S activity during cln5 - growth and starvation. (frontiersin.org)
  • A hallmark of proteome balance is the ubiquitin-proteasome system (UPS) that degrades roughly 80% of multi-ubiquitinated proteins ( Collins and Goldberg, 2017 ). (elifesciences.org)
  • We found that Homer3, the predominant isoform in Purkinje cells, is phosphorylated by calcium/calmodulin-dependent protein kinase II (CaMKII) both in vitro and in vivo . (jneurosci.org)
  • In this study, we revealed that Homer3 was phosphorylated by calcium/calmodulin-dependent protein kinase II (CaMKII) in Purkinje cells, and the phosphorylation reduces the affinity for Homer target molecules, resulting in change of the solubility. (jneurosci.org)
  • Protein kinase D1 (PKD1), together with PKD2 and PKD3, constitute a family classified within the calcium/calmodulin-dependent protein kinase superfamily 7 . (nature.com)
  • Unlike other calcium channel accessory subunits which increase calcium current, when coexpressed with the Cav1 Foretinib clinical trial 1 was demonstrated to accelerate L kind calcium current activation and inactivation in heterologous programs. (plcsignaling.com)
  • Given the similarities in sequence and tissue distribution between 1 and 6, it appeared likely that the 6 subunit might tell 1 an ability to modulate myocyte calcium current. (plcsignaling.com)
  • The other sub-units within cardiac myocytes do not cause an inhibition of Cav3 dependent calcium present, a finding that's consistent with the prediction that the 6 subunit shares with 1 unique functional consequences on myocyte calcium channels. (plcsignaling.com)
  • In this study,we extend the electrophysiological analysis of 6 to show that the protein regulates LVA calcium current in native cardiac myocytes as well as in cell lines and to identify important sequences and structural features within the 6 subunit that are involved in its modulation of LVA calcium current. (plcsignaling.com)
  • Adaptor protein-2 (AP2), a central component of clathrin-coated vesicles (CCVs), is pivotal in clathrin-mediated endocytosis, which internalizes plasma membrane constituents such as G protein-coupled receptors (GPCRs). (ox.ac.uk)
  • AP2 is chiefly involved in endocytosis of cell surface proteins and their trafficking to early or late endosomes. (eu.org)
  • The DNA-binding motifs suggest this protein is involved in the regulation of transcription and chromatin remodeling. (wikipedia.org)
  • AP2, a heterotetramer of α, β, μ and σ subunits, links clathrin to vesicle membranes and binds to tyrosine- and dileucine-based motifs of membrane-associated cargo proteins. (ox.ac.uk)
  • The latter dileucine motifs were implicated in membrane protein sorting to vacuoles or tonoplasts. (eu.org)
  • In fungi and plants, dileucine motifs are often responsible for the vacuolar or tonoplast localization of proteins carrying these motifs. (eu.org)
  • Co appearance of Gefitinib EGFR inhibitor the 6 subunit duplicated from cardiac muscle with 3. (plcsignaling.com)
  • Biochemical reconstitution demonstrates that the mammalian complex possesses inherent E3 ubiquitin ligase activity, using Ube2H as its cognate E2. (elifesciences.org)
  • PsA generates stiffness, pain, Sigma-1 receptor antagonist 2 and swelling of bones, and it can progress to debilitating joint damage. (kinasechem.com)
  • While earlier reports found earlier age groups of onset and higher risks of systemic swelling in individuals with IL36RN mutations [14], more recent studies have shown no difference in disease severity Sigma-1 receptor antagonist 2 between individuals with IL36RN solitary heterozygous mutations and homozygous or compound heterozygous mutations [18,19]. (kinasechem.com)
  • To further complicate this matter, a significant association of IL-36RN mutations with early age of Sigma-1 receptor antagonist 2 onset, regardless of phenotype, was found in a recent study including 863 individuals with pustular psoriasis [17,20]. (kinasechem.com)
  • Recently, we isolated a novel negative regulator of epidermal growth factor receptor (EGFR), termed EGFR-related protein (ERRP), whose expression attenuates EGFR activation. (aacrjournals.org)
  • The citric type, pin-pointed a available interface( complex), describes an Second subcellular transcription within a receptor path-finding. (evakoch.com)
  • Both 1 and 6 have short C terminal regions that lack the consensus PDZ1 binding motif that is a distinctive characteristic of the four subunits known collectively because the TARP proteins Chromoblastomycosis that control AMPA receptor trafficking and function. (plcsignaling.com)
  • The main structural coat protein of COATED VESICLES which play a key role in the intracellular transport between membranous organelles. (lookformedical.com)
  • Additional genes with mutations associated with pustular psoriasis include caspase-activating recruitment website member 14 (Cards14), adaptor protein complex 1 subunit sigma 3 (AP1S3), TNFAIP3-interacting protein 1 (TNIP1), and serpin family A member 3 (SERPINA 3) [16]. (kinasechem.com)
  • IQSEC2: encodes an exchange factor for the Arf family of small GTP binding proteins, involved in the formation of secretory vesicles. (wikipedia.org)
  • TM4SF2: is a member of the 4 transmembrane domains family of proteins (tetraspanins, see TSPAN7). (wikipedia.org)
  • ZNF41: Zinc finger protein 41 is a likely zinc finger family transcription factor. (wikipedia.org)
  • FTSJ1: Transfert RNA methyltransferase 1 is a member of the S-adenosylmethionine-binding protein family. (wikipedia.org)
  • GDI1: RabGDI alpha makes a complex with geranylgeranylated small GTP-binding proteins of the Rab family and keeps them in the cytosol. (wikipedia.org)
  • It is a member of the group-II aristaless-related protein family whose members are expressed primarily in the central and/or peripheral nervous system. (wikipedia.org)
  • KDM5C: Lysine-specific demethylase 5C is an enzyme that in humans is encoded by the KDM5C gene a member of the SMCY homolog family and encodes a protein with one ARID domain, one JmjC domain, one JmjN domain and two PHD-type zinc fingers. (wikipedia.org)
  • PHF8: PHD finger protein 8 belongs to the family of ferrous iron and 2-oxoglutarate dependent oxygenases, and is a histone lysine demethylase with selectivity for the di-and monomethyl states. (wikipedia.org)
  • FMR2: Fragile mental retardation 2 (FMR2: synonym AFF2), the protein belongs to the AFF family which currently has four members: AFF1/AF4, AFF2/FMR2, AFF3/LAF4 and AFF4/AF5q31. (wikipedia.org)
  • A family of proteins that play a role as cofactors in the process of CLATHRIN recycling in cells. (lookformedical.com)
  • The initial member of this protein family to be identified, 1, was isolated like a subunit of the high-voltage activated, Cav1. (plcsignaling.com)
  • Phylogenetic and sequence homology analysis suggests that the recently described 6 protein may be the closest homologue of just one inside the family. (plcsignaling.com)
  • family Poxviridae , subfamily Chordopoxvirinae , genus Orthopoxvirus ) are complex, double-stranded DNA viruses with ongoing interest because of their potential use as bioterrorism agents and in gene therapy. (cdc.gov)
  • MipA is an immunoreactive protein [ 6 ] that belongs to a family of proteins involved in remodeling peptidoglycan. (biomedcentral.com)
  • on chromosome 19q13.3, which encodes the adaptor-related protein complex 2 sigma (AP2σ) subunit, cause FHH type 3. (ox.ac.uk)
  • 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)
  • During growth, genes associated with protein ubiquitination/deubiquitination, cell cycle progression, and proteasomal degradation were affected, while genes linked to protein and carbohydrate catabolism were affected during early development. (frontiersin.org)
  • Overall, this study reveals the impact of cln5 -deficiency on gene expression in D. discoideum , provides insight on the genes and proteins that play a role in regulating Cln5-dependent processes, and sheds light on the molecular mechanisms underlying CLN5 disease. (frontiersin.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)
  • They preferentially bind and release hydrophobic peptides by an ATP-dependent process and are involved in post-translational PROTEIN TRANSLOCATION. (lookformedical.com)
  • RNA enzymes may observe from also translocated proteins, they may phosphorylate suggested in proteins with delayed strategies, or they may outline known in membranes of factor factors. (evakoch.com)
  • Integrin-linked kinase (ILK) is a major structural adaptor protein governing signaling complex formation and cytoskeletal dynamics. (jneurosci.org)
  • Clathrin also interacts with cytoskeletal proteins. (lookformedical.com)
  • MECP2: methyl CpG binding protein 2 is a transcription regulator, which represses transcription from methylated gene promoters. (wikipedia.org)
  • subunit alpha of MPP mitochondrial signal peptidase heterodimer","protein_coding" "Zm00001e017599_P001","No alias","Zea mays","Protein disulfide isomerase-like 2-2 OS=Oryza sativa subsp. (ntu.edu.sg)
  • A constitutively expressed subfamily of the HSP70 heat-shock proteins. (lookformedical.com)
  • Adaptor protein complex 1 is found on the cytoplasmic face of vesicles located at the Golgi complex, where it mediates both the recruitment of clathrin to the membrane and the recognition of sorting signals within the cytosolic tails of transmembrane receptors. (wikipedia.org)
  • SYP7 group Qc-type SNARE protein","protein_coding" "MA_10436714g0010","No alias","Picea abies","acyl-CoA thioesterase","protein_coding" "MA_135972g0010","No alias","Picea abies","Acyl-CoA-binding domain-containing protein 3 OS=Oryza sativa subsp. (ntu.edu.sg)
  • 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. (lookformedical.com)
  • In complexes, the other enzymes affect cleaved CBF1( or RBPJkappa), while in channels they are required Lag-1, immediately that the m ' CSL ' demonstrates separated been to this produced feature experience breast. (evakoch.com)
  • preferentially, post-translational amino-acid JmjC increases are activated provided and conserved to regulate pentose cell polysaccharides with antimicrobial program protein and Clot positions. (erik-mill.de)
  • 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. (lookformedical.com)
  • A clathrin adaptor protein complex primarily involved in clathrin-related transport at the TRANS-GOLGI NETWORK. (lookformedical.com)
  • 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)
  • Specialized regions of the cell membrane composed of pits coated with a bristle covering made of the protein CLATHRIN. (lookformedical.com)
  • An adaptor protein complex primarily involved in the formation of clathrin-related endocytotic vesicles (ENDOSOMES) at the CELL MEMBRANE. (lookformedical.com)
  • 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. (lookformedical.com)
  • 14) strand proteins in gene-internal of FGFR3 and capable sunshine amyloid or proteotoxic cell increasing( Otsuki, 1999). (evakoch.com)
  • Our biochemical and cellular analysis thus demonstrates that the GID/CTLH complex prevents cell cycle exit in G1, at least in part by degrading Hbp1. (elifesciences.org)
  • Cellular proteostasis involves the coordinated and compensatory action of pathways that control biogenesis, folding, trafficking and breakdown of proteins allowing the cell to adapt to physiological or pathological environmental changes. (elifesciences.org)
  • The proteins of such MAPKs increased and were then repress UniProt differential download Sarkozy, Israël et whereby steps include to the spliced group before any further cell. (erik-mill.de)
  • The outer surface of these vesicles is covered with a lattice-like network of the protein CLATHRIN. (lookformedical.com)
  • A class of proteins involved in the transport of molecules via TRANSPORT VESICLES. (lookformedical.com)
  • A broad category of proteins involved in the formation, transport and dissolution of TRANSPORT VESICLES. (lookformedical.com)
  • By developing a holistic approach to tackle the complexity of interactions, we decipher the complex intra-host interactions underlying Pacific oyster mortality syndrome affecting juveniles of Crassostrea gigas , the main oyster species exploited worldwide. (nature.com)
  • The objective of the present work was to examine one disease of complex aetiology affecting one of the most utilized invertebrate species in the world, the Pacific oyster Crassostrea gigas , applying a holistic approach to decipher the phenomenon. (nature.com)
  • The MLH and MutL ketoacyl-CoA species extend with complexes of MutS analyses to exchange signal subsequent effects. (erik-mill.de)
  • The pathway maps illustrate protein interactions and regulation to provide a comprehensive picture of signaling and disease processes. (bio-rad.com)
  • Lamellipodial protrusion and directional migration of carcinoma cells towards chemoattractants, such as epidermal growth factor (EGF), depend upon the spatial and temporal regulation of actin cytoskeleton by actin-binding proteins (ABPs). (rupress.org)
  • Psoriatic arthritis (PsA) is definitely a complex inflammatory joint disease included in the spondyloarthropathy spectrum that affects approximately one-third of psoriasis individuals, especially those with moderate-to-severe psoriasis [7]. (kinasechem.com)
  • Unexpectedly, we find that excitotoxicity provokes an early inactivation of PKD1 through a dephosphorylation-dependent mechanism mediated by protein phosphatase-1 (PP1) and dual specificity phosphatase-1 (DUSP1). (nature.com)
  • neuroendocrine convertase 2 precursor like status:Partially_confirmed UniProt:P91863 protein_id:CAB0. (yeastrc.org)
  • The steps of infantile sites linked and represented extensively form UniProt ECM-associated gene whereby effects circulate to the associated building before any further complex. (erik-mill.de)
  • 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)
  • Introduced to France in the 1970s, C . gigas suffers mass mortalities associated with complex interactions between the host, the environment and pathogens 5 . (nature.com)