Dynamin binds to SH3 domains of phospholipase C gamma and GRB-2
Src homology 3 (SH3) domains are found in a variety of proteins that are involved in signal transduction or represent components of the cytoskeleton. These domains are thought to serve as modules that mediate specific protein-protein interactions that include proline-rich sequences on the target pro...
Saved in:
Published in | The Journal of biological chemistry Vol. 269; no. 23; pp. 16009 - 16014 |
---|---|
Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Bethesda, MD
American Society for Biochemistry and Molecular Biology
10.06.1994
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Summary: | Src homology 3 (SH3) domains are found in a variety of proteins that are involved in signal transduction or represent components
of the cytoskeleton. These domains are thought to serve as modules that mediate specific protein-protein interactions that
include proline-rich sequences on the target protein. We have identified proteins of 110, 80, 65, and 43 kDa in human embryonic
fibroblasts that bind specifically to the SH3 domain of phospholipase C gamma, a primary substrate of receptor tyrosine kinases,
and characterized the 110-kDa band as the microtubule-activated GTPase dynamin. In addition, dynamin binds the son of sevenless
adaptor protein GRB-2 with even higher affinity. This interaction does not require the dynamin GTPase function and involves
a proline-rich target sequence between residues 812 and 820 of dynamin. |
---|---|
Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/S0021-9258(17)33965-0 |