WASF2

From Wikipedia, the free encyclopedia

WAS protein family, member 2

PDB rendering based on 2a40.

Available structures: 2a40

Identifiers

Symbol(s)

WASF2; SCAR2; WAVE2; dJ393P12.2

External IDs

OMIM: 605875 HomoloGene: 86920

Gene ontology
Molecular Function:	• actin binding • histamine receptor activity
Cellular Component:	• cytoskeleton • actin cytoskeleton • integral to membrane
Biological Process:	• G-protein coupled receptor protein signaling pathway • G-protein signaling, coupled to cAMP nucleotide second messenger • actin cytoskeleton organization and biogenesis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

n/a

Refseq

NM_006990 (mRNA)
NP_008921 (protein)

n/a (mRNA)
n/a (protein)

Location

Chr 1: 27.6 - 27.69 Mb

n/a

Pubmed search

[1]

n/a

WAS protein family, member 2, also known as WASF2, is a human gene.

This gene encodes a member of the Wiskott-Aldrich syndrome protein family. The gene product is a protein that forms a multiprotein complex that links receptor kinases and actin. Binding to actin occurs through a C-terminal verprolin homology domain in all family members. The multiprotein complex serves to tranduce signals that involve changes in cell shape, motility or function. The published map location (PMID:10381382) has been changed based on recent genomic sequence comparisons, which indicate that the expressed gene is located on chromosome 1, and a pseudogene may be located on chromosome X.^[1]

[edit] References

^ Entrez Gene: WASF2 WAS protein family, member 2.

[edit] Further reading

Jones GE (2000). "Cellular signaling in macrophage migration and chemotaxis.". J. Leukoc. Biol. 68 (5): 593–602. PMID 11073096.
She HY, Rockow S, Tang J, et al. (1997). "Wiskott-Aldrich syndrome protein is associated with the adapter protein Grb2 and the epidermal growth factor receptor in living cells.". Mol. Biol. Cell 8 (9): 1709–21. PMID 9307968.
Bear JE, Rawls JF, Saxe CL (1998). "SCAR, a WASP-related protein, isolated as a suppressor of receptor defects in late Dictyostelium development.". J. Cell Biol. 142 (5): 1325–35. PMID 9732292.
Wu Y, Dowbenko D, Lasky LA (1998). "PSTPIP 2, a second tyrosine phosphorylated, cytoskeletal-associated protein that binds a PEST-type protein-tyrosine phosphatase.". J. Biol. Chem. 273 (46): 30487–96. PMID 9804817.
Machesky LM, Insall RH (1999). "Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex.". Curr. Biol. 8 (25): 1347–56. PMID 9889097.
Qualmann B, Roos J, DiGregorio PJ, Kelly RB (1999). "Syndapin I, a synaptic dynamin-binding protein that associates with the neural Wiskott-Aldrich syndrome protein.". Mol. Biol. Cell 10 (2): 501–13. PMID 9950691.
Stewart DM, Tian L, Nelson DL (1999). "Mutations that cause the Wiskott-Aldrich syndrome impair the interaction of Wiskott-Aldrich syndrome protein (WASP) with WASP interacting protein.". J. Immunol. 162 (8): 5019–24. PMID 10202051.
Suetsugu S, Miki H, Takenawa T (1999). "Identification of two human WAVE/SCAR homologues as general actin regulatory molecules which associate with the Arp2/3 complex.". Biochem. Biophys. Res. Commun. 260 (1): 296–302. doi:10.1006/bbrc.1999.0894. PMID 10381382.
Morrogh LM, Hinshelwood S, Costello P, et al. (1999). "The SH3 domain of Bruton's tyrosine kinase displays altered ligand binding properties when auto-phosphorylated in vitro.". Eur. J. Immunol. 29 (7): 2269–79. PMID 10427990.
Banin S, Gout I, Brickell P (1999). "Interaction between Wiskott-Aldrich Syndrome protein (WASP) and the Fyn protein-tyrosine kinase.". Mol. Biol. Rep. 26 (3): 173–7. PMID 10532312.
Westphal RS, Soderling SH, Alto NM, et al. (2000). "Scar/WAVE-1, a Wiskott-Aldrich syndrome protein, assembles an actin-associated multi-kinase scaffold.". EMBO J. 19 (17): 4589–600. doi:10.1093/emboj/19.17.4589. PMID 10970852.
Miki H, Yamaguchi H, Suetsugu S, Takenawa T (2001). "IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling.". Nature 408 (6813): 732–5. doi:10.1038/35047107. PMID 11130076.
Marchand JB, Kaiser DA, Pollard TD, Higgs HN (2001). "Interaction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex.". Nat. Cell Biol. 3 (1): 76–82. doi:10.1038/35050590. PMID 11146629.
Millard TH, Machesky LM (2001). "The Wiskott-Aldrich syndrome protein (WASP) family.". Trends Biochem. Sci. 26 (3): 198–9. PMID 11246027.
Worby CA, Simonson-Leff N, Clemens JC, et al. (2002). "Drosophila Ack targets its substrate, the sorting nexin DSH3PX1, to a protein complex involved in axonal guidance.". J. Biol. Chem. 277 (11): 9422–8. doi:10.1074/jbc.M110172200. PMID 11773052.
Miki H, Takenawa T (2002). "WAVE2 serves a functional partner of IRSp53 by regulating its interaction with Rac.". Biochem. Biophys. Res. Commun. 293 (1): 93–9. doi:10.1016/S0006-291X(02)00218-8. PMID 12054568.
Eden S, Rohatgi R, Podtelejnikov AV, et al. (2002). "Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck.". Nature 418 (6899): 790–3. doi:10.1038/nature00859. PMID 12181570.
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.
Innocenti M, Zucconi A, Disanza A, et al. (2004). "Abi1 is essential for the formation and activation of a WAVE2 signalling complex.". Nat. Cell Biol. 6 (4): 319–27. doi:10.1038/ncb1105. PMID 15048123.