| 释义 |
- Interactions
- References
- Further reading
- External links
{{Infobox_gene}}Wiskott-Aldrich syndrome protein family member 2 is a protein that in humans is encoded by the WASF2 gene.[1]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.[2] InteractionsWASF2 has been shown to interact with BAIAP2.[3] References1. ^{{cite journal |vauthors=Suetsugu S, Miki H, Takenawa T | title = Identification of two human WAVE/SCAR homologues as general actin regulatory molecules which associate with the Arp2/3 complex | journal = Biochem Biophys Res Commun | volume = 260 | issue = 1 | pages = 296–302 | date=July 1999| pmid = 10381382 | pmc = | doi = 10.1006/bbrc.1999.0894 }}
2. ^{{cite web | title = Entrez Gene: WASF2 WAS protein family, member 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10163| accessdate = }}
3. ^{{cite journal |last=Miki |first=H |authorlink= |author2=Yamaguchi H |author3=Suetsugu S |author4=Takenawa T |date=December 2000|title=IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling |journal=Nature |volume=408 |issue=6813 |pages=732–5 | issn = 0028-0836| pmid = 11130076 |doi = 10.1038/35047107 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}
Further reading{{refbegin | 2}}- {{cite journal | author=Jones GE |title=Cellular signaling in macrophage migration and chemotaxis. |journal=J. Leukoc. Biol. |volume=68 |issue= 5 |pages= 593–602 |year= 2000 |pmid= 11073096 |doi= }}
- {{cite journal |vauthors=She HY, Rockow S, Tang J, etal |title=Wiskott-Aldrich syndrome protein is associated with the adapter protein Grb2 and the epidermal growth factor receptor in living cells. |journal=Mol. Biol. Cell |volume=8 |issue= 9 |pages= 1709–21 |year= 1997 |pmid= 9307968 |doi= 10.1091/mbc.8.9.1709| pmc=305731 }}
- {{cite journal |vauthors=Bear JE, Rawls JF, Saxe CL |title=SCAR, a WASP-related protein, isolated as a suppressor of receptor defects in late Dictyostelium development. |journal=J. Cell Biol. |volume=142 |issue= 5 |pages= 1325–35 |year= 1998 |pmid= 9732292 |doi=10.1083/jcb.142.5.1325 | pmc=2149354 }}
- {{cite journal |vauthors=Wu Y, Dowbenko D, Lasky LA |title=PSTPIP 2, a second tyrosine phosphorylated, cytoskeletal-associated protein that binds a PEST-type protein-tyrosine phosphatase. |journal=J. Biol. Chem. |volume=273 |issue= 46 |pages= 30487–96 |year= 1998 |pmid= 9804817 |doi=10.1074/jbc.273.46.30487 }}
- {{cite journal |vauthors=Machesky LM, Insall RH |title=Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex. |journal=Curr. Biol. |volume=8 |issue= 25 |pages= 1347–56 |year= 1999 |pmid= 9889097 |doi=10.1016/S0960-9822(98)00015-3 }}
- {{cite journal |vauthors=Qualmann B, Roos J, DiGregorio PJ, Kelly RB |title=Syndapin I, a synaptic dynamin-binding protein that associates with the neural Wiskott-Aldrich syndrome protein. |journal=Mol. Biol. Cell |volume=10 |issue= 2 |pages= 501–13 |year= 1999 |pmid= 9950691 |doi= 10.1091/mbc.10.2.501| pmc=25183 }}
- {{cite journal |vauthors=Stewart DM, Tian L, Nelson DL |title=Mutations that cause the Wiskott-Aldrich syndrome impair the interaction of Wiskott-Aldrich syndrome protein (WASP) with WASP interacting protein. |journal=J. Immunol. |volume=162 |issue= 8 |pages= 5019–24 |year= 1999 |pmid= 10202051 |doi= }}
- {{cite journal |vauthors=Morrogh LM, Hinshelwood S, Costello P, etal |title=The SH3 domain of Bruton's tyrosine kinase displays altered ligand binding properties when auto-phosphorylated in vitro. |journal=Eur. J. Immunol. |volume=29 |issue= 7 |pages= 2269–79 |year= 1999 |pmid= 10427990 |doi=10.1002/(SICI)1521-4141(199907)29:07<2269::AID-IMMU2269>3.0.CO;2-# }}
- {{cite journal |vauthors=Banin S, Gout I, Brickell P |title=Interaction between Wiskott-Aldrich Syndrome protein (WASP) and the Fyn protein-tyrosine kinase. |journal=Mol. Biol. Rep. |volume=26 |issue= 3 |pages= 173–7 |year= 1999 |pmid= 10532312 |doi=10.1023/A:1006954206151 }}
- {{cite journal |vauthors=Westphal RS, Soderling SH, Alto NM, etal |title=Scar/WAVE-1, a Wiskott-Aldrich syndrome protein, assembles an actin-associated multi-kinase scaffold. |journal=EMBO J. |volume=19 |issue= 17 |pages= 4589–600 |year= 2000 |pmid= 10970852 |doi= 10.1093/emboj/19.17.4589 | pmc=302050 }}
- {{cite journal |vauthors=Miki H, Yamaguchi H, Suetsugu S, Takenawa T |title=IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling. |journal=Nature |volume=408 |issue= 6813 |pages= 732–5 |year= 2001 |pmid= 11130076 |doi= 10.1038/35047107 }}
- {{cite journal |vauthors=Marchand JB, Kaiser DA, Pollard TD, Higgs HN |title=Interaction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex. |journal=Nat. Cell Biol. |volume=3 |issue= 1 |pages= 76–82 |year= 2001 |pmid= 11146629 |doi= 10.1038/35050590 }}
- {{cite journal |vauthors=Millard TH, Machesky LM |title=The Wiskott-Aldrich syndrome protein (WASP) family. |journal=Trends Biochem. Sci. |volume=26 |issue= 3 |pages= 198–9 |year= 2001 |pmid= 11246027 |doi=10.1016/S0968-0004(01)01788-1 }}
- {{cite journal |vauthors=Worby CA, Simonson-Leff N, Clemens JC, etal |title=Drosophila Ack targets its substrate, the sorting nexin DSH3PX1, to a protein complex involved in axonal guidance. |journal=J. Biol. Chem. |volume=277 |issue= 11 |pages= 9422–8 |year= 2002 |pmid= 11773052 |doi= 10.1074/jbc.M110172200 }}
- {{cite journal |vauthors=Miki H, Takenawa T |title=WAVE2 serves a functional partner of IRSp53 by regulating its interaction with Rac. |journal=Biochem. Biophys. Res. Commun. |volume=293 |issue= 1 |pages= 93–9 |year= 2002 |pmid= 12054568 |doi= 10.1016/S0006-291X(02)00218-8 }}
- {{cite journal |vauthors=Eden S, Rohatgi R, Podtelejnikov AV, etal |title=Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck. |journal=Nature |volume=418 |issue= 6899 |pages= 790–3 |year= 2002 |pmid= 12181570 |doi= 10.1038/nature00859 |bibcode=2002Natur.418..790E }}
- {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |bibcode=2002PNAS...9916899M }}
- {{cite journal |vauthors=Innocenti M, Zucconi A, Disanza A, etal |title=Abi1 is essential for the formation and activation of a WAVE2 signalling complex. |journal=Nat. Cell Biol. |volume=6 |issue= 4 |pages= 319–27 |year= 2004 |pmid= 15048123 |doi= 10.1038/ncb1105 }}
{{refend}}External links- {{UCSC genome browser|WASF2}}
- {{UCSC gene details|WASF2}}
{{PDB Gallery|geneid=10163}}{{gene-1-stub}} |