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 Druker, Thomas M. Roberts, Qi An, Lan Bo Chen

Research output: Contribution to journalArticle

155 Citations (Scopus)

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 Ab1, Fps, Src, and Src family members, the transforming protein Crk, phospholipase C-γy1, PI-3 (phosphatidylinositol) kinase, and guanosine triphosphatase-activating protein (GAP). Like the SH2 domain found in Src, Crk, and Ab1, 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.

Original languageEnglish (US)
Pages (from-to)712-715
Number of pages4
JournalScience
Volume252
Issue number5006
StatePublished - May 3 1991
Externally publishedYes

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Microfilament Proteins
src Homology Domains
Phosphotyrosine
Protein-Tyrosine Kinases
Actins
Signal Transduction
Oncogene Protein pp60(v-src)
Proteins
Focal Adhesions
Guanosine
Molecular Cloning
Type C Phospholipases
Phosphatidylinositols
Cytoskeleton
Phosphatidylinositol 3-Kinases
Tyrosine
Amino Acid Sequence
Complementary DNA
Tensins

ASJC Scopus subject areas

  • General

Cite this

Davis, S., Lu, M. L., Lo, S. H., Lin, S., Butler, J. A., Druker, B., ... Chen, L. B. (1991). Presence of an SH2 domain in the actin-binding protein tensin. Science, 252(5006), 712-715.

Presence of an SH2 domain in the actin-binding protein tensin. / Davis, Samuel; Lu, Michael L.; Lo, Su Hao; Lin, Shin; Butler, James A.; Druker, Brian; Roberts, Thomas M.; An, Qi; Chen, Lan Bo.

In: Science, Vol. 252, No. 5006, 03.05.1991, p. 712-715.

Research output: Contribution to journalArticle

Davis, S, Lu, ML, Lo, SH, Lin, S, Butler, JA, Druker, B, Roberts, TM, An, Q & Chen, LB 1991, 'Presence of an SH2 domain in the actin-binding protein tensin', Science, vol. 252, no. 5006, pp. 712-715.
Davis S, Lu ML, Lo SH, Lin S, Butler JA, Druker B et al. Presence of an SH2 domain in the actin-binding protein tensin. Science. 1991 May 3;252(5006):712-715.
Davis, Samuel ; Lu, Michael L. ; Lo, Su Hao ; Lin, Shin ; Butler, James A. ; Druker, Brian ; Roberts, Thomas M. ; An, Qi ; Chen, Lan Bo. / Presence of an SH2 domain in the actin-binding protein tensin. In: Science. 1991 ; Vol. 252, No. 5006. pp. 712-715.
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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 Ab1, Fps, Src, and Src family members, the transforming protein Crk, phospholipase C-γy1, PI-3 (phosphatidylinositol) kinase, and guanosine triphosphatase-activating protein (GAP). Like the SH2 domain found in Src, Crk, and Ab1, 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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AU - Roberts, Thomas M.

AU - An, Qi

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N2 - 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 Ab1, Fps, Src, and Src family members, the transforming protein Crk, phospholipase C-γy1, PI-3 (phosphatidylinositol) kinase, and guanosine triphosphatase-activating protein (GAP). Like the SH2 domain found in Src, Crk, and Ab1, 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.

AB - 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 Ab1, Fps, Src, and Src family members, the transforming protein Crk, phospholipase C-γy1, PI-3 (phosphatidylinositol) kinase, and guanosine triphosphatase-activating protein (GAP). Like the SH2 domain found in Src, Crk, and Ab1, 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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