Presence of an SH2 domain in the actin-binding protein tensin

Samuel Davis, Michael L. Lu, Su Hao Lo, Shin Lin, James A. Butler, Brian J. Druker, Thomas M. Roberts, Qi An, Lan Bo Chen

Research output: Contribution to journalArticlepeer-review

17 Scopus citations


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-γl, 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 phosphotyrosinebinding activities and being itself a target for tyrosine kinases, tensin may link signal transduction pathways with the cytoskeleton.

Original languageEnglish (US)
Pages (from-to)712-715
Number of pages4
Issue number5006
StatePublished - 1991
Externally publishedYes

ASJC Scopus subject areas

  • General


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