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Presence of an SH2 Domain in the Actin-Binding Protein Tensin
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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Cited by
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Schaller, M. D., Borgman, C. A., Cobb, B. S., Vines, R. R., Reynolds, A. B., & Parsons, J. T. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.11.5192 · Cited by 1,444
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Metadata
- Authors
- Davis, S., Lu, M. L., Lo, S. H., Lin, S., Butler, J. A., Druker, B. J., Roberts, T. M., An, Q., & Chen, L. B.
- Venue
- Science
- Published
- 1991-05-03
- Volume
- 252
- Issue
- 5006
- Pages
- 712-715
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2085154580
- Cited by
- 251
- References
- 0
- FWCI
- 14.08
- Type
- journal article
- Language
- en
- Open access
- closed
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- Davis, S., Lu, M. L., Lo, S. H., Lin, S., Butler, J. A., Druker, B. J., Roberts, T. M., An, Q., & Chen, L. B. (1991). Presence of an SH2 Domain in the Actin-Binding Protein Tensin. Science. https://doi.org/10.1126/science.1708917
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