PMID: 9655255Jul 9, 1998Paper

Formation of a stable src-AFAP-110 complex through either an amino-terminal or a carboxy-terminal SH2-binding motif

Molecular Carcinogenesis
A C GuapponeDaniel C Flynn

Abstract

The actin-filament-associated protein (AFAP-1 10) forms a stable complex with activated variants of the Pp60c-src (Src) non-receptor tyrosine kinase through SH2 and SH3 interactions. In this report, site-directed mutagenesis and a transient expression system that permits co-expression of activated pp60c-src (Src527F) and AFAP-110 in Cos-1 cells were used to identify the SH2-binding motif in AFAP-110. Four tyrosine residues, two in the amino terminus (Y93 and Y94) and two in the carboxy terminus (Y451 and Y453), were mutated to phenylalanine, significantly reducing overall steady-state levels of tyrosine phosphorylation and preventing Src527F from forming a stable complex with AFAP-110. These data indicate that the major sites for tyrosine phosphorylation are among these four tyrosine residues and that one or more of these tyrosines may function as an SH2-binding motif. Mutagenesis of just two tyrosines in either the amino terminus (Y93/Y94) or in the carboxy terminus (Y451/Y453) to phenylalanine had only a modest effect on steady-state levels of tyrosine phosphorylation and was not sufficient to abrogate stable-complex formation. These data suggest that Src527F can form a stable complex with AFAP-110 through either of two indep...Continue Reading

References

Jun 1, 1992·Proceedings of the National Academy of Sciences of the United States of America·M D SchallerJ T Parsons
May 1, 1990·Proceedings of the National Academy of Sciences of the United States of America·S B KannerJ T Parsons
Nov 1, 1990·Proceedings of the National Academy of Sciences of the United States of America·M F MoranT Pawson
Sep 1, 1989·Molecular and Cellular Biology·A B ReynoldsJ T Parsons
Aug 1, 1987·Molecular and Cellular Biology·C Chen, H Okayama
Feb 1, 1982·Proceedings of the National Academy of Sciences of the United States of America·T PatschinskyB M Sefton
Mar 1, 1994·Molecular and Cellular Biology·M D SchallerJ T Parsons
Apr 28, 1994·Nature·S FumagalliS A Courtneidge
Mar 12, 1993·Cell·Z SongyangR J Lechleider
Apr 28, 1995·The Journal of Biological Chemistry·G AlonsoS A Courtneidge
Jan 1, 1996·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·S J Taylor, D Shalloway
Apr 12, 1996·The Journal of Biological Chemistry·T NakamotoH Hirai

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Citations

Jul 23, 2002·Molecular Biology of the Cell·Yong QianDaniel C Flynn
Aug 18, 2004·Molecular and Cellular Biology·Amanda GatesmanDaniel C Flynn
Oct 19, 2001·Oncogene·S A Weed, J T Parsons
Jul 13, 2002·American Journal of Physiology. Lung Cellular and Molecular Physiology·Monika LodygaMingyao Liu
Jan 18, 2003·Journal of Neurobiology·David A ClumpDaniel C Flynn
Oct 16, 2004·The Journal of Biological Chemistry·Bing HanMingyao Liu
Jun 21, 2016·International Journal of Molecular Sciences·Yujian ChenShaojun Liu
May 24, 2007·Journal of Cellular Physiology·Andrea DorfleutnerDaniel C Flynn
Oct 15, 2013·Oncogene·A B ReynoldsJ T Parsons
Jun 26, 2008·Journal of Cell Science·Andrea DorfleutnerDaniel C Flynn
Mar 14, 2009·Differentiation; Research in Biological Diversity·Xiaohua XuLorene M Lanier
Feb 22, 2011·European Journal of Cell Biology·Brandi N SnyderJess M Cunnick
May 10, 2011·Current Opinion in Cell Biology·Olivier DestaingCorinne Albiges-Rizo

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