AP2A1

From Wikipedia, the free encyclopedia

Adaptor-related protein complex 2, alpha 1 subunit

PDB rendering based on 1gw5.

Available structures: 1gw5

Identifiers

Symbol(s)

AP2A1; ADTAA; AP2-ALPHA; CLAPA1

External IDs

OMIM: 601026 MGI: 101921 HomoloGene: 68997

Gene ontology
Molecular Function:	• structural molecule activity • protein binding
Cellular Component:	• coated pit • membrane coat • AP-2 adaptor complex • clathrin coat of trans-Golgi network vesicle
Biological Process:	• protein complex assembly • intracellular protein transport • Golgi to endosome transport • endocytosis

Orthologs

Human

Mouse

Refseq

NM_014203 (mRNA)
NP_055018 (protein)

XM_001002959 (mRNA)
XP_001002959 (protein)

Location

Chr 19: 54.96 - 55 Mb

Chr 7: 44.77 - 44.8 Mb

Pubmed search

[1]

[2]

Adaptor-related protein complex 2, alpha 1 subunit, also known as AP2A1, is a human gene.

This gene encodes the alpha 1 adaptin subunit of the adaptor protein 2 (AP-2) complex found in clathrin coated vesicles. The AP-2 complex is a heterotetramer consisting of two large adaptins (alpha or beta), a medium adaptin (mu), and a small adaptin (sigma). The complex is part of the protein coat on the cytoplasmic face of coated vesicles which links clathrin to receptors in vesicles. Alternative splicing of this gene results in two transcript variants encoding two different isoforms. A third transcript variant has been described, but its full length nature has not been determined.^[1]

[edit] References

^ Entrez Gene: AP2A1 adaptor-related protein complex 2, alpha 1 subunit.

[edit] Further reading

Kirchhausen T (2000). "Clathrin.". Annu. Rev. Biochem. 69: 699–727. doi:10.1146/annurev.biochem.69.1.699. PMID 10966473.
Robinson MS (1989). "Cloning of cDNAs encoding two related 100-kD coated vesicle proteins (alpha-adaptins).". J. Cell Biol. 108 (3): 833–42. PMID 2564002.
Goodman OB, Keen JH (1995). "The alpha chain of the AP-2 adaptor is a clathrin binding subunit.". J. Biol. Chem. 270 (40): 23768–73. PMID 7559550.
Page LJ, Robinson MS (1995). "Targeting signals and subunit interactions in coated vesicle adaptor complexes.". J. Cell Biol. 131 (3): 619–30. PMID 7593184.
Li C, Ullrich B, Zhang JZ, et al. (1995). "Ca(2+)-dependent and -independent activities of neural and non-neural synaptotagmins.". Nature 375 (6532): 594–9. doi:10.1038/375594a0. PMID 7791877.
Okabayashi Y, Sugimoto Y, Totty NF, et al. (1996). "Interaction of Shc with adaptor protein adaptins.". J. Biol. Chem. 271 (9): 5265–9. PMID 8617812.
Benmerah A, Bégue B, Dautry-Varsat A, Cerf-Bensussan N (1996). "The ear of alpha-adaptin interacts with the COOH-terminal domain of the Eps 15 protein.". J. Biol. Chem. 271 (20): 12111–6. PMID 8662627.
van Delft S, Schumacher C, Hage W, et al. (1997). "Association and colocalization of Eps15 with adaptor protein-2 and clathrin.". J. Cell Biol. 136 (4): 811–21. PMID 9049247.
McMahon HT, Wigge P, Smith C (1997). "Clathrin interacts specifically with amphiphysin and is displaced by dynamin.". FEBS Lett. 413 (2): 319–22. PMID 9280305.
Chen H, Fre S, Slepnev VI, et al. (1998). "Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis.". Nature 394 (6695): 793–7. doi:10.1038/29555. PMID 9723620.
Berlioz-Torrent C, Shacklett BL, Erdtmann L, et al. (1999). "Interactions of the cytoplasmic domains of human and simian retroviral transmembrane proteins with components of the clathrin adaptor complexes modulate intracellular and cell surface expression of envelope glycoproteins.". J. Virol. 73 (2): 1350–61. PMID 9882340.
Hussain NK, Yamabhai M, Ramjaun AR, et al. (1999). "Splice variants of intersectin are components of the endocytic machinery in neurons and nonneuronal cells.". J. Biol. Chem. 274 (22): 15671–7. PMID 10336464.
Tebar F, Bohlander SK, Sorkin A (1999). "Clathrin assembly lymphoid myeloid leukemia (CALM) protein: localization in endocytic-coated pits, interactions with clathrin, and the impact of overexpression on clathrin-mediated traffic.". Mol. Biol. Cell 10 (8): 2687–702. PMID 10436022.
Vleurick L, Pezet A, Kühn ER, et al. (1999). "A beta-turn endocytic code is required for optimal internalization of the growth hormone receptor but not for alpha-adaptin association.". Mol. Endocrinol. 13 (11): 1823–31. PMID 10551776.
Fan GH, Yang W, Wang XJ, et al. (2001). "Identification of a motif in the carboxyl terminus of CXCR2 that is involved in adaptin 2 binding and receptor internalization.". Biochemistry 40 (3): 791–800. PMID 11170396.
Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.". Genome Res. 11 (3): 422–35. doi:10.1101/gr.154701. PMID 11230166.
Sakaguchi K, Okabayashi Y, Kasuga M (2001). "Shc mediates ligand-induced internalization of epidermal growth factor receptors.". Biochem. Biophys. Res. Commun. 282 (5): 1154–60. doi:10.1006/bbrc.2001.4680. PMID 11302736.
Crump CM, Xiang Y, Thomas L, et al. (2001). "PACS-1 binding to adaptors is required for acidic cluster motif-mediated protein traffic.". EMBO J. 20 (9): 2191–201. doi:10.1093/emboj/20.9.2191. PMID 11331585.
Rotem-Yehudar R, Galperin E, Horowitz M (2001). "Association of insulin-like growth factor 1 receptor with EHD1 and SNAP29.". J. Biol. Chem. 276 (35): 33054–60. doi:10.1074/jbc.M009913200. PMID 11423532.