Heteronuclear NMR Studies of the Combined Src Homology Domains 2 and 3 of pp60 c-Src:  Effects of Phosphopeptide Binding†

Biochemistry ◽  
1997 ◽  
Vol 36 (47) ◽  
pp. 14561-14571 ◽  
Author(s):  
Marco Tessari ◽  
Lisa N. Gentile ◽  
Stephen J. Taylor ◽  
David I. Shalloway ◽  
Linda K. Nicholson ◽  
...  
Keyword(s):  
Heteronuclear Nmr ◽  
Nmr Studies ◽  
Src Homology ◽  
Src Homology Domains ◽  
Homology Domains

scholarly journals Inhibition of VRAC by c-Src tyrosine kinase targeted to caveolae is mediated by the Src homology domains

2001 ◽  
Vol 281 (1) ◽  
pp. C248-C256 ◽  
Author(s):  
Dominique Trouet ◽  
Iris Carton ◽  
Diane Hermans ◽  
Guy Droogmans ◽  
Bernd Nilius ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Inhibitory Effect ◽  
Kinase Domain ◽  
Wild Type ◽  
Patch Clamp Technique ◽  
Src Tyrosine Kinase ◽  
Src Homology ◽  
Cpae Cells ◽  
Src Homology Domains ◽  
Homology Domains

We used the whole cell patch-clamp technique in calf pulmonary endothelial (CPAE) cells to investigate the effect of wild-type and mutant c-Src tyrosine kinase on I Cl,swell, the swelling-induced Cl−current through volume-regulated anion channels (VRAC). Transient transfection of wild-type c-Src in CPAE cells did not significantly affect I Cl,swell. However, transfection of c-Src with a Ser3Cys mutation that introduces a dual acylation signal and targets c-Src to lipid rafts and caveolae strongly repressed hypotonicity-induced I Cl,swell in CPAE cells. Kinase activity was dispensable for the inhibition of I Cl,swell, since kinase-deficient c-Src Ser3Cys either with an inactivating point mutation in the kinase domain or with the entire kinase domain deleted still suppressed VRAC activity. Again, the Ser3Cys mutation was required to obtain maximal inhibition by the kinase-deleted c-Src. In contrast, the inhibitory effect was completely lost when the Src homology domains 2 and 3 were deleted in c-Src. We therefore conclude that c-Src-mediated inhibition of VRAC requires compartmentalization of c-Src to caveolae and that the Src homology domains 2 and/or 3 are necessary and sufficient for inhibition.

scholarly journals Src Homology Domains of Phospholipase C γ1 Inhibit Nerve Growth Factor-Induced Differentiation of PC12 Cells

2002 ◽  
Vol 71 (1) ◽  
pp. 178-185 ◽  
Author(s):  
Sun Sik Bae ◽  
Young Han Lee ◽  
Jong-Soo Chang ◽  
Sehamuddin H. Galadari ◽  
Yong Sik Kim ◽  
...  
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Phospholipase C ◽  
Pc12 Cells ◽  
Induced Differentiation ◽  
Nerve Growth ◽  
Src Homology ◽  
Src Homology Domains ◽  
Homology Domains

scholarly journals Cooperation of Src Homology Domains in the Regulated Binding of Phosphatidylinositol 3-Kinase

1995 ◽  
Vol 270 (14) ◽  
pp. 7937-7943 ◽  
Author(s):  
Burkhard Haefner ◽  
Ruth Baxter ◽  
Valerie J. Fincham ◽  
C. Peter Downes ◽  
Margaret C. Frame
Keyword(s):  
Phosphatidylinositol 3 Kinase ◽  
Src Homology ◽  
Src Homology Domains ◽  
Phosphatidylinositol 3 ◽  
Homology Domains
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