CRKL

From Wikipedia, the free encyclopedia

V-crk sarcoma virus CT10 oncogene homolog (avian)-like

PDB rendering based on 2bzx.

Available structures: 2bzx, 2bzy, 2dbk

Identifiers

Symbol(s)

CRKL;

External IDs

OMIM: 602007 MGI: 104686 HomoloGene: 38021

Gene ontology
Molecular Function:	• protein-tyrosine kinase activity • SH3/SH2 adaptor activity • protein binding
Biological Process:	• protein amino acid phosphorylation • cell motility • intracellular signaling cascade • JNK cascade • Ras protein signal transduction • organ morphogenesis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_005207 (mRNA)
NP_005198 (protein)

NM_007764 (mRNA)
NP_031790 (protein)

Location

Chr 22: 19.6 - 19.64 Mb

Chr 16: 17.37 - 17.4 Mb

Pubmed search

[1]

[2]

V-crk sarcoma virus CT10 oncogene homolog (avian)-like, also known as CRKL, is a human gene.

v-CRK avian sarcoma virus CT10-homolog-like contains one SH2 domain and two SH3 domains. CRKL has been shown to activate the RAS and JUN kinase signaling pathways and transform fibroblasts in a RAS-dependent fashion. It is a substrate of the BCR-ABL tyrosine kinase and plays a role in fibroblast transformation by BCR-ABL. In addition, CRKL has oncogenic potential.^[1]

[edit] References

^ Entrez Gene: CRKL v-crk sarcoma virus CT10 oncogene homolog (avian)-like.

[edit] Further reading

Feller SM, Posern G, Voss J, et al. (1999). "Physiological signals and oncogenesis mediated through Crk family adapter proteins.". J. Cell. Physiol. 177 (4): 535–52. doi:10.1002/(SICI)1097-4652(199812)177:4<535::AID-JCP5>3.0.CO;2-E. PMID 10092207.
Salgia R, Uemura N, Okuda K, et al. (1996). "CRKL links p210BCR/ABL with paxillin in chronic myelogenous leukemia cells.". J. Biol. Chem. 270 (49): 29145–50. PMID 7493940.
Ren R, Ye ZS, Baltimore D (1994). "Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites.". Genes Dev. 8 (7): 783–95. PMID 7926767.
Oda T, Heaney C, Hagopian JR, et al. (1994). "Crkl is the major tyrosine-phosphorylated protein in neutrophils from patients with chronic myelogenous leukemia.". J. Biol. Chem. 269 (37): 22925–8. PMID 8083188.
ten Hoeve J, Morris C, Heisterkamp N, Groffen J (1993). "Isolation and chromosomal localization of CRKL, a human crk-like gene.". Oncogene 8 (9): 2469–74. PMID 8361759.
Smit L, van der Horst G, Borst J (1996). "Sos, Vav, and C3G participate in B cell receptor-induced signaling pathways and differentially associate with Shc-Grb2, Crk, and Crk-L adaptors.". J. Biol. Chem. 271 (15): 8564–9. PMID 8621483.
Senechal K, Halpern J, Sawyers CL (1996). "The CRKL adaptor protein transforms fibroblasts and functions in transformation by the BCR-ABL oncogene.". J. Biol. Chem. 271 (38): 23255–61. PMID 8798523.
Salgia R, Pisick E, Sattler M, et al. (1996). "p130CAS forms a signaling complex with the adapter protein CRKL in hematopoietic cells transformed by the BCR/ABL oncogene.". J. Biol. Chem. 271 (41): 25198–203. PMID 8810278.
Ingham RJ, Krebs DL, Barbazuk SM, et al. (1997). "B cell antigen receptor signaling induces the formation of complexes containing the Crk adapter proteins.". J. Biol. Chem. 271 (50): 32306–14. PMID 8943292.
Heaney C, Kolibaba K, Bhat A, et al. (1997). "Direct binding of CRKL to BCR-ABL is not required for BCR-ABL transformation.". Blood 89 (1): 297–306. PMID 8978305.
Manié SN, Beck AR, Astier A, et al. (1997). "Involvement of p130(Cas) and p105(HEF1), a novel Cas-like docking protein, in a cytoskeleton-dependent signaling pathway initiated by ligation of integrin or antigen receptor on human B cells.". J. Biol. Chem. 272 (7): 4230–6. PMID 9020138.
de Jong R, ten Hoeve J, Heisterkamp N, Groffen J (1997). "Tyrosine 207 in CRKL is the BCR/ABL phosphorylation site.". Oncogene 14 (5): 507–13. doi:10.1038/sj.onc.1200885. PMID 9053848.
Uemura N, Salgia R, Li JL, et al. (1997). "The BCR/ABL oncogene alters interaction of the adapter proteins CRKL and CRK with cellular proteins.". Leukemia 11 (3): 376–85. PMID 9067577.
Sattler M, Salgia R, Shrikhande G, et al. (1997). "Steel factor induces tyrosine phosphorylation of CRKL and binding of CRKL to a complex containing c-kit, phosphatidylinositol 3-kinase, and p120(CBL).". J. Biol. Chem. 272 (15): 10248–53. PMID 9092574.
Sattler M, Salgia R, Shrikhande G, et al. (1997). "Differential signaling after beta1 integrin ligation is mediated through binding of CRKL to p120(CBL) and p110(HEF1).". J. Biol. Chem. 272 (22): 14320–6. PMID 9162067.
Husson H, Mograbi B, Schmid-Antomarchi H, et al. (1997). "CSF-1 stimulation induces the formation of a multiprotein complex including CSF-1 receptor, c-Cbl, PI 3-kinase, Crk-II and Grb2.". Oncogene 14 (19): 2331–8. doi:10.1038/sj.onc.1201074. PMID 9178909.
Chin H, Saito T, Arai A, et al. (1997). "Erythropoietin and IL-3 induce tyrosine phosphorylation of CrkL and its association with Shc, SHP-2, and Cbl in hematopoietic cells.". Biochem. Biophys. Res. Commun. 239 (2): 412–7. doi:10.1006/bbrc.1997.7480. PMID 9344843.
Ahmad S, Alsayed YM, Druker BJ, Platanias LC (1997). "The type I interferon receptor mediates tyrosine phosphorylation of the CrkL adaptor protein.". J. Biol. Chem. 272 (48): 29991–4. PMID 9374471.
de Jong R, van Wijk A, Haataja L, et al. (1998). "BCR/ABL-induced leukemogenesis causes phosphorylation of Hef1 and its association with Crkl.". J. Biol. Chem. 272 (51): 32649–55. PMID 9405482.
Gesbert F, Garbay C, Bertoglio J (1998). "Interleukin-2 stimulation induces tyrosine phosphorylation of p120-Cbl and CrkL and formation of multimolecular signaling complexes in T lymphocytes and natural killer cells.". J. Biol. Chem. 273 (7): 3986–93. PMID 9461587.