Difference between revisions of "Phosphatase Subfamily Tensin"
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===Evolution=== | ===Evolution=== | ||
| − | Tensins are found throughout holozoa. Drosophilids have a truncated ortholog (''blistery'') which lacks the phosphatase domain, though the full-length form is seen in mosquitoes. One of the four human members, TNS4, is also truncated. | + | Tensins are found throughout holozoa. Drosophilids have a truncated ortholog ([http://www.sdbonline.org/sites/fly/cytoskel/blistery1.htm ''blistery'']) which lacks the phosphatase domain, though the full-length form is seen in mosquitoes. One of the four human members, TNS4, is also truncated. |
===Domain Structure=== | ===Domain Structure=== | ||
Revision as of 04:56, 28 December 2014
Phosphatase Classification: Superfamily CC1: Family PTEN: Subfamily Tensin
Tensins are PTEN-related phosphatases involved in integrin signaling.
Evolution
Tensins are found throughout holozoa. Drosophilids have a truncated ortholog (blistery) which lacks the phosphatase domain, though the full-length form is seen in mosquitoes. One of the four human members, TNS4, is also truncated.
Domain Structure
Tensins are long proteins, with an N-terminal phosphatase domain followed immediately by a PTEN_C2 domain, which acts as a lipid-binding domain. They have a poorly conserved middle region and and SH2 and usually PTB domains at the C-terminus. Human TENC1 and the sponge Tensin also have an N-terminal C1 domain. Humans also have a homologous TENC4 protein which is N-terminally truncated and has lost the phosphatase domain. The phosphatase domain is divergent and not picked by by many domain tools.
Functions
Tensin are localized to integrin-mediated focal adhesions. The PTB domain binds to the cytoplasmic region of integrins, and they bind actin through an N-terminal region. SH2 domains interact with a variety of tyrosine-phosphorylated proteins, including PI3K, FAK, and p130Cas. The catalytic functions of the phosphatase domain are not well understood. TNS2 (TENC1) induced in vivo dephosporylation of phosphatidylinositol 3,4,5-trisphosphate, though the activity could not be replaced in vitro [1]. Another report[2] showed TNS2 protein tyrosine phosphatase activity on IRS-1
References
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