Adapter molecule crk also known as proto-oncogene c-Crk is a
protein that in humans is encoded by the CRKgene.[5]
The CRK protein participates in the
Reelin signaling cascade downstream of
DAB1.[6][7]
Function
Adapter molecule crk is a member of an
adapter protein family that binds to several tyrosine-phosphorylated proteins. This protein 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.[8]
Crk together with
CrkL participates in the
Reelin signaling cascade downstream of
DAB1.[6][7]
v-Crk, a transforming oncoprotein from avian sarcoma viruses, is a fusion of viral "gag" protein with the SH2 and SH3 domains of cellular Crk.[9] The name Crk is from "CT10 Regulator of Kinase" where CT10 is the avian virus from which was isolated a protein, lacking kinase domains, but capable of stimulating phosphorylation of tyrosines in cells.[10]
Crk should not be confused with
Src, which also has cellular (c-Src) and viral (v-Src) forms and is involved in some of the same signaling pathways but is a protein tyrosine-kinase.
^Wang JF, Park IW, Groopman JE (2000). "Stromal cell-derived factor-1alpha stimulates tyrosine phosphorylation of multiple focal adhesion proteins and induces migration of hematopoietic progenitor cells: roles of phosphoinositide-3 kinase and protein kinase C". Blood. 95 (8): 2505–13.
doi:
10.1182/blood.V95.8.2505.
PMID10753828.
^
abMatsumoto T, Yokote K, Take A, Takemoto M, Asaumi S, Hashimoto Y, Matsuda M, Saito Y, Mori S (2000). "Differential interaction of CrkII adaptor protein with platelet-derived growth factor alpha- and beta-receptors is determined by its internal tyrosine phosphorylation". Biochem. Biophys. Res. Commun. 270 (1): 28–33.
doi:
10.1006/bbrc.2000.2374.
PMID10733900.
Cicchetti P, Mayer BJ, Thiel G, Baltimore D (1992). "Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho". Science. 257 (5071): 803–6.
Bibcode:
1992Sci...257..803C.
doi:
10.1126/science.1379745.
PMID1379745.
Adapter molecule crk also known as proto-oncogene c-Crk is a
protein that in humans is encoded by the CRKgene.[5]
The CRK protein participates in the
Reelin signaling cascade downstream of
DAB1.[6][7]
Function
Adapter molecule crk is a member of an
adapter protein family that binds to several tyrosine-phosphorylated proteins. This protein 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.[8]
Crk together with
CrkL participates in the
Reelin signaling cascade downstream of
DAB1.[6][7]
v-Crk, a transforming oncoprotein from avian sarcoma viruses, is a fusion of viral "gag" protein with the SH2 and SH3 domains of cellular Crk.[9] The name Crk is from "CT10 Regulator of Kinase" where CT10 is the avian virus from which was isolated a protein, lacking kinase domains, but capable of stimulating phosphorylation of tyrosines in cells.[10]
Crk should not be confused with
Src, which also has cellular (c-Src) and viral (v-Src) forms and is involved in some of the same signaling pathways but is a protein tyrosine-kinase.
^Wang JF, Park IW, Groopman JE (2000). "Stromal cell-derived factor-1alpha stimulates tyrosine phosphorylation of multiple focal adhesion proteins and induces migration of hematopoietic progenitor cells: roles of phosphoinositide-3 kinase and protein kinase C". Blood. 95 (8): 2505–13.
doi:
10.1182/blood.V95.8.2505.
PMID10753828.
^
abMatsumoto T, Yokote K, Take A, Takemoto M, Asaumi S, Hashimoto Y, Matsuda M, Saito Y, Mori S (2000). "Differential interaction of CrkII adaptor protein with platelet-derived growth factor alpha- and beta-receptors is determined by its internal tyrosine phosphorylation". Biochem. Biophys. Res. Commun. 270 (1): 28–33.
doi:
10.1006/bbrc.2000.2374.
PMID10733900.
Cicchetti P, Mayer BJ, Thiel G, Baltimore D (1992). "Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho". Science. 257 (5071): 803–6.
Bibcode:
1992Sci...257..803C.
doi:
10.1126/science.1379745.
PMID1379745.