Adapter molecule crk

Adapter molecule crk also known as proto-oncogene c-Crk is a protein that in humans is encoded by the CRK gene.[5]

CRK
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCRK, CRKII, p38, v-crk avian sarcoma virus CT10 oncogene homolog, CRK proto-oncogene, adaptor protein
External IDsOMIM: 164762 MGI: 88508 HomoloGene: 81850 GeneCards: CRK
Gene location (Human)
Chr.Chromosome 17 (human)[1]
Band17p13.3Start1,420,689 bp[1]
End1,463,162 bp[1]
RNA expression pattern




More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

1398

12928

Ensembl

ENSG00000167193

ENSMUSG00000017776

UniProt

P46108

Q64010

RefSeq (mRNA)

NM_016823
NM_005206

NM_001277219
NM_001277221
NM_133656

RefSeq (protein)

NP_005197
NP_058431

NP_001264148
NP_001264150
NP_598417

Location (UCSC)Chr 17: 1.42 – 1.46 MbChr 11: 75.68 – 75.71 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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.

Interactions

CRK (gene) has been shown to interact with:

See also
  • CrkL, "Crk-like" protein

References
  1. GRCh38: Ensembl release 89: ENSG00000167193 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000017776 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Mayer BJ, Hanafusa H (1990). "Association of the v-crk oncogene product with phosphotyrosine-containing proteins and protein kinase activity". Proc Natl Acad Sci U S A. 87 (7): 2638–42. Bibcode:1990PNAS...87.2638M. doi:10.1073/pnas.87.7.2638. PMC 53745. PMID 1690891.
  6. Matsuki T, Pramatarova A, Howell BW (June 2008). "Reduction of Crk and CrkL expression blocks reelin-induced dendritogenesis". J. Cell Sci. 121 (Pt 11): 1869–75. doi:10.1242/jcs.027334. PMC 2430739. PMID 18477607.
  7. Park TJ, Curran T (December 2008). "Crk and Crk-like play essential overlapping roles downstream of disabled-1 in the Reelin pathway". J. Neurosci. 28 (50): 13551–62. doi:10.1523/JNEUROSCI.4323-08.2008. PMC 2628718. PMID 19074029.
  8. "Entrez Gene: CRK v-crk sarcoma virus CT10 oncogene homolog (avian)".
  9. Tetsuya Nakamoto; Ryuichi Sakai; Keiya Ozawa; Yoshio Yazaki; Hisamaru Hirai (1996). "Direct Binding of C-terminal Region of p130Graphic to SH2 and SH3 Domains of Src Kinase". J. Biol. Chem. 271 (15): 8959–8965. doi:10.1074/jbc.271.15.8959. PMID 8621540.
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Further reading
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