CD2AP

From Wikipedia, the free encyclopedia

CD2-associated protein

PDB rendering based on 2j6f.

Available structures: 2j6f, 2j6k, 2j6o, 2j7i

Identifiers

Symbol(s)

CD2AP; CMS; DKFZP586H0519

External IDs

OMIM: 604241 MGI: 1330281 HomoloGene: 7663

Gene ontology
Molecular Function:	• structural constituent of cytoskeleton • protein binding • SH3 domain binding
Cellular Component:	• ruffle • cytoplasm • actin cytoskeleton • filamentous actin
Biological Process:	• protein complex assembly • substrate-bound cell migration, cell extension • signal transduction

Orthologs

Human

Mouse

Refseq

NM_012120 (mRNA)
NP_036252 (protein)

NM_009847 (mRNA)
NP_033977 (protein)

Location

Chr 6: 47.55 - 47.7 Mb

Chr 17: 42.26 - 42.32 Mb

Pubmed search

[1]

[2]

CD2-associated protein, also known as CD2AP, is a human gene.^[1]

This gene encodes a scaffolding molecule that regulates the actin cytoskeleton. The protein directly interacts with filamentous actin and a variety of cell membrane proteins through multiple actin binding sites, SH3 domains, and a proline-rich region containing binding sites for SH3 domains. The cytoplasmic protein localizes to membrane ruffles, lipid rafts, and the leading edges of cells. It is implicated in dynamic actin remodeling and membrane trafficking that occurs during receptor endocytosis and cytokinesis. Haploinsufficiency of this gene is implicated in susceptibility to glomerular disease.^[1]

[edit] References

^ ^a ^b Entrez Gene: CD2AP CD2-associated protein.

[edit] Further reading

Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. PMID 8889548.
Dustin ML, Olszowy MW, Holdorf AD, et al. (1998). "A novel adaptor protein orchestrates receptor patterning and cytoskeletal polarity in T-cell contacts.". Cell 94 (5): 667–77. PMID 9741631.
Kirsch KH, Georgescu MM, Ishimaru S, Hanafusa H (1999). "CMS: an adapter molecule involved in cytoskeletal rearrangements.". Proc. Natl. Acad. Sci. U.S.A. 96 (11): 6211–6. PMID 10339567.
Lehtonen S, Ora A, Olkkonen VM, et al. (2000). "In vivo interaction of the adapter protein CD2-associated protein with the type 2 polycystic kidney disease protein, polycystin-2.". J. Biol. Chem. 275 (42): 32888–93. doi:10.1074/jbc.M006624200. PMID 10913159.
Li C, Ruotsalainen V, Tryggvason K, et al. (2000). "CD2AP is expressed with nephrin in developing podocytes and is found widely in mature kidney and elsewhere.". Am. J. Physiol. Renal Physiol. 279 (4): F785–92. PMID 10997929.
Kirsch KH, Georgescu MM, Shishido T, et al. (2001). "The adapter type protein CMS/CD2AP binds to the proto-oncogenic protein c-Cbl through a tyrosine phosphorylation-regulated Src homology 3 domain interaction.". J. Biol. Chem. 276 (7): 4957–63. doi:10.1074/jbc.M005784200. PMID 11067845.
Schwarz K, Simons M, Reiser J, et al. (2002). "Podocin, a raft-associated component of the glomerular slit diaphragm, interacts with CD2AP and nephrin.". J. Clin. Invest. 108 (11): 1621–9. PMID 11733557.
Scott MP, Zappacosta F, Kim EY, et al. (2002). "Identification of novel SH3 domain ligands for the Src family kinase Hck. Wiskott-Aldrich syndrome protein (WASP), WASP-interacting protein (WIP), and ELMO1.". J. Biol. Chem. 277 (31): 28238–46. doi:10.1074/jbc.M202783200. PMID 12029088.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Badour K, Zhang J, Shi F, et al. (2003). "The Wiskott-Aldrich syndrome protein acts downstream of CD2 and the CD2AP and PSTPIP1 adaptors to promote formation of the immunological synapse.". Immunity 18 (1): 141–54. PMID 12530983.
Cormont M, Metón I, Mari M, et al. (2003). "CD2AP/CMS regulates endosome morphology and traffic to the degradative pathway through its interaction with Rab4 and c-Cbl.". Traffic 4 (2): 97–112. PMID 12559036.
Lynch DK, Winata SC, Lyons RJ, et al. (2003). "A Cortactin-CD2-associated protein (CD2AP) complex provides a novel link between epidermal growth factor receptor endocytosis and the actin cytoskeleton.". J. Biol. Chem. 278 (24): 21805–13. doi:10.1074/jbc.M211407200. PMID 12672817.
Hutchings NJ, Clarkson N, Chalkley R, et al. (2003). "Linking the T cell surface protein CD2 to the actin-capping protein CAPZ via CMS and CIN85.". J. Biol. Chem. 278 (25): 22396–403. doi:10.1074/jbc.M302540200. PMID 12690097.
Kim JM, Wu H, Green G, et al. (2003). "CD2-associated protein haploinsufficiency is linked to glomerular disease susceptibility.". Science 300 (5623): 1298–300. doi:10.1126/science.1081068. PMID 12764198.
Schulze WX, Mann M (2004). "A novel proteomic screen for peptide-protein interactions.". J. Biol. Chem. 279 (11): 10756–64. doi:10.1074/jbc.M309909200. PMID 14679214.
Haglund K, Ivankovic-Dikic I, Shimokawa N, et al. (2004). "Recruitment of Pyk2 and Cbl to lipid rafts mediates signals important for actin reorganization in growing neurites.". J. Cell. Sci. 117 (Pt 12): 2557–68. doi:10.1242/jcs.01148. PMID 15128873.
Lehtonen S, Lehtonen E, Kudlicka K, et al. (2004). "Nephrin forms a complex with adherens junction proteins and CASK in podocytes and in Madin-Darby canine kidney cells expressing nephrin.". Am. J. Pathol. 165 (3): 923–36. PMID 15331416.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455.
Coward RJ, Foster RR, Patton D, et al. (2005). "Nephrotic plasma alters slit diaphragm-dependent signaling and translocates nephrin, Podocin, and CD2 associated protein in cultured human podocytes.". J. Am. Soc. Nephrol. 16 (3): 629–37. doi:10.1681/ASN.2004030172. PMID 15659563.