Open AccessDeletions in the SH2 domain of p60v-src prevent association with the detergent-insoluble cellular matrix.
Author(s) -
Yoshinori Fukui,
M C O'Brien,
Hidesaburô Hanafusa
Publication year - 1991
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.11.3.1207
Subject(s) - proto oncogene tyrosine protein kinase src , biology , autophosphorylation , sh3 domain , sh2 domain , protein kinase domain , microbiology and biotechnology , kinase , biochemistry , mutant , tyrosine protein kinase csk , protein kinase a , gene
p60v-src has been shown to associate with a detergent-insoluble cellular matrix containing cytoskeletal proteins, but p60c-src does not bind to this matrix. We analyzed the association of mutant src proteins with the matrix and found that mutants which lack an amino-terminal portion (residues 149 to 169) of the SH2 domain cannot bind to the matrix. Neither the SH3 region nor other portions of the SH2 region were required for association. We also tested protein kinase-defective mutants and chimeras of p60v-src and p60c-src. We found a strong correlation between the kinase activity of p60src and its association with the detergent-insoluble matrix. Double infection of kinase-defective and kinase-active mutants did not result in matrix binding of the kinase-defective src proteins. We also found that Tyr-416, the major site of autophosphorylation in p60v-src, was not required for matrix association.