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Multiple Grb2‐protein complexes in human cancer cells
Author(s) -
Sastry Lakshmi,
Cao Tin,
King C. Richter
Publication year - 1997
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/(sici)1097-0215(19970117)70:2<208::aid-ijc12>3.0.co;2-e
Subject(s) - grb2 , sh3 domain , sh2 domain , signal transducing adaptor protein , proto oncogene tyrosine protein kinase src , biology , receptor tyrosine kinase , tyrosine kinase , phosphotyrosine binding domain , microbiology and biotechnology , cancer research , egf like domain , signal transduction , biochemistry , binding domain , binding site
Grb2 is an SH2/SH3 domain‐containing adaptor protein that links receptor tyrosine kinases to the ras signaling pathway. The Grb2‐SH2 domain binds phosphotyrosine sequences on activated tyrosine kinases, and one target of the SH3 domains is the ras ‐nucleotide‐exchange factor Sos1. We have examined Grb2‐protein interactions in human cancer cells that over‐express the receptor tyrosine kinase erbB2. Our results show that the 2 Grb2‐SH3 domains complex with Sos1, dynamin and at least 4 other proteins (p228, p140, p55, p28) in these cells. The 2 Grb2‐SH3 domains bind these proteins differently, with the N‐terminal SH3 domain interacting preferentially with p228, Sos1, p140 and dynamin. The C‐terminal SH3 domain has higher affinity toward p28. The Grb2‐SH3 domain interactions appear to be similar in erbB2 over‐expressing breast, ovarian and lung cancer cells. Also, the major tyrosine‐phosphorylated proteins that associate with Grb2 in erbB2 over‐expressing cancer cells appear to be erbB2 and Shc. The multiple Grb2‐SH3 domain interactions in these cells may mediate novel cellular functions. Int. J. Cancer, 70:208–213, 1977. © 1997 Wiley‐Liss Inc.

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