CRK (gene)

CRK is a gene which codes a protein exhibiting the SH2 domain.

PBB_Summary
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summary_text = This gene encodes a member of an adapter protein family that binds to several tyrosine-phosphorylated proteins. The product of this gene has several SH2 and SH3 domains (src-homology domains) and is involved in several signaling pathways, recruiting cytoplasmic proteins in the vicinity of tyrosine kinase through SH2-phosphotyrosine interaction. The N-terminal SH2 domain of this protein functions as a positive regulator of transformation whereas the C-terminal SH3 domain functions as a negative regulator of transformation. Two alternative transcripts encoding different isoforms with distinct biological activity have been described. [cite web | title = Entrez Gene: CRK v-crk sarcoma virus CT10 oncogene homolog (avian)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1398| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Feller SM, Ren R, Hanafusa H, Baltimore D |title=SH2 and SH3 domains as molecular adhesives: the interactions of Crk and Abl. |journal=Trends Biochem. Sci. |volume=19 |issue= 11 |pages= 453–8 |year= 1995 |pmid= 7855886 |doi=
*cite journal | author=Feller SM, Posern G, Voss J, "et al." |title=Physiological signals and oncogenesis mediated through Crk family adapter proteins. |journal=J. Cell. Physiol. |volume=177 |issue= 4 |pages= 535–52 |year= 1999 |pmid= 10092207 |doi= 10.1002/(SICI)1097-4652(199812)177:4<535::AID-JCP5>3.0.CO;2-E |doilabel=10.1002/(SICI)1097-4652(199812)177:4535::AID-JCP53.0.CO;2-E
*cite journal | author=Pessin JE, Okada S |title=Insulin and EGF receptors integrate the Ras and Rap signaling pathways. |journal=Endocr. J. |volume=46 Suppl |issue= |pages= S11–6 |year= 2002 |pmid= 12054111 |doi=
*cite journal | author=Cicchetti P, Mayer BJ, Thiel G, Baltimore D |title=Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho. |journal=Science |volume=257 |issue= 5071 |pages= 803–6 |year= 1992 |pmid= 1379745 |doi=
*cite journal | author=Matsuda M, Tanaka S, Nagata S, "et al." |title=Two species of human CRK cDNA encode proteins with distinct biological activities. |journal=Mol. Cell. Biol. |volume=12 |issue= 8 |pages= 3482–9 |year= 1992 |pmid= 1630456 |doi=
*cite journal | author=Mayer BJ, Hanafusa H |title=Association of the v-crk oncogene product with phosphotyrosine-containing proteins and protein kinase activity. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 7 |pages= 2638–42 |year= 1990 |pmid= 1690891 |doi=
*cite journal | author=Anderson D, Koch CA, Grey L, "et al." |title=Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors. |journal=Science |volume=250 |issue= 4983 |pages= 979–82 |year= 1990 |pmid= 2173144 |doi=
*cite journal | author=Schaller MD, Hildebrand JD, Shannon JD, "et al." |title=Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src. |journal=Mol. Cell. Biol. |volume=14 |issue= 3 |pages= 1680–8 |year= 1994 |pmid= 7509446 |doi=
*cite journal | author=Hempstead BL, Birge RB, Fajardo JE, "et al." |title=Expression of the v-crk oncogene product in PC12 cells results in rapid differentiation by both nerve growth factor- and epidermal growth factor-dependent pathways. |journal=Mol. Cell. Biol. |volume=14 |issue= 3 |pages= 1964–71 |year= 1994 |pmid= 7509449 |doi=
*cite journal | author=Tanaka S, Morishita T, Hashimoto Y, "et al." |title=C3G, a guanine nucleotide-releasing protein expressed ubiquitously, binds to the Src homology 3 domains of CRK and GRB2/ASH proteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 8 |pages= 3443–7 |year= 1994 |pmid= 7512734 |doi=
*cite journal | author=Calalb MB, Polte TR, Hanks SK |title=Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases. |journal=Mol. Cell. Biol. |volume=15 |issue= 2 |pages= 954–63 |year= 1995 |pmid= 7529876 |doi=
*cite journal | author=Teng KK, Lander H, Fajardo JE, "et al." |title=v-Crk modulation of growth factor-induced PC12 cell differentiation involves the Src homology 2 domain of v-Crk and sustained activation of the Ras/mitogen-activated protein kinase pathway. |journal=J. Biol. Chem. |volume=270 |issue= 35 |pages= 20677–85 |year= 1995 |pmid= 7657647 |doi=
*cite journal | author=Schumacher C, Knudsen BS, Ohuchi T, "et al." |title=The SH3 domain of Crk binds specifically to a conserved proline-rich motif in Eps15 and Eps15R. |journal=J. Biol. Chem. |volume=270 |issue= 25 |pages= 15341–7 |year= 1995 |pmid= 7797522 |doi=
*cite journal | author=Matsuda M, Hashimoto Y, Muroya K, "et al." |title=CRK protein binds to two guanine nucleotide-releasing proteins for the Ras family and modulates nerve growth factor-induced activation of Ras in PC12 cells. |journal=Mol. Cell. Biol. |volume=14 |issue= 8 |pages= 5495–500 |year= 1994 |pmid= 8035825 |doi=
*cite journal | author=Feller SM, Knudsen B, Hanafusa H |title=c-Abl kinase regulates the protein binding activity of c-Crk. |journal=EMBO J. |volume=13 |issue= 10 |pages= 2341–51 |year= 1994 |pmid= 8194526 |doi=
*cite journal | author=Fioretos T, Heisterkamp N, Groffen J, "et al." |title=CRK proto-oncogene maps to human chromosome band 17p13. |journal=Oncogene |volume=8 |issue= 10 |pages= 2853–5 |year= 1993 |pmid= 8378094 |doi=
*cite journal | author=Smit L, van der Horst G, Borst J |title=Sos, Vav, and C3G participate in B cell receptor-induced signaling pathways and differentially associate with Shc-Grb2, Crk, and Crk-L adaptors. |journal=J. Biol. Chem. |volume=271 |issue= 15 |pages= 8564–9 |year= 1996 |pmid= 8621483 |doi=
*cite journal | author=Beitner-Johnson D, Blakesley VA, Shen-Orr Z, "et al." |title=The proto-oncogene product c-Crk associates with insulin receptor substrate-1 and 4PS. Modulation by insulin growth factor-I (IGF) and enhanced IGF-I signaling. |journal=J. Biol. Chem. |volume=271 |issue= 16 |pages= 9287–90 |year= 1996 |pmid= 8621590 |doi=
*cite journal | author=Hasegawa H, Kiyokawa E, Tanaka S, "et al." |title=DOCK180, a major CRK-binding protein, alters cell morphology upon translocation to the cell membrane. |journal=Mol. Cell. Biol. |volume=16 |issue= 4 |pages= 1770–6 |year= 1996 |pmid= 8657152 |doi=

External links

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