Abstract
The molecular cloning of the complementary DNA coding for a 90-kilodalton fragment of tensin, an actin-binding component of focal contacts and other submembraneous cytoskeletal structures, is reported. The derived amino acid sequence revealed the presence of a Src homology 2 (SH2) domain. This domain is shared by a number of signal transduction proteins including nonreceptor tyrosine kinases such as Abl, Fps, Src, and Src family members, the transforming protein Crk, phospholipase C-γ1, PI-3 (phosphatidylinositol) kinase, and guanosine triphosphatase-activating protein (GAP). Like the SH2 domain found in Src, Crk, and Abl, the SH2 domain of tensin bound specifically to a number of phosphotyrosine-containing proteins from v-src-transformed cells. Tensin was also found to be phosphorylated on tyrosine residues. These findings suggest that by possessing both actin-binding and phosphotyrosine-binding activities and being itself a target for tyrosine kinases, tensin may link signal transduction pathways with the cytoskeleton.
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Dates
Type | When |
---|---|
Created | 18 years, 10 months ago (Oct. 5, 2006, 6:10 p.m.) |
Deposited | 1 year, 7 months ago (Jan. 11, 2024, 11:40 a.m.) |
Indexed | 3 months, 2 weeks ago (May 12, 2025, 10:46 a.m.) |
Issued | 34 years, 3 months ago (May 3, 1991) |
Published | 34 years, 3 months ago (May 3, 1991) |
Published Print | 34 years, 3 months ago (May 3, 1991) |
@article{Davis_1991, title={Presence of an SH2 Domain in the Actin-Binding Protein Tensin}, volume={252}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.1708917}, DOI={10.1126/science.1708917}, number={5006}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Davis, Samuel and Lu, Michael L. and Lo, Su Hao and Lin, Shin and Butler, James A. and Druker, Brian J. and Roberts, Thomas M. and An, Qi and Chen, Lan Bo}, year={1991}, month=may, pages={712–715} }