Tensin


Glossary Term: Tensin


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Tensin is essential for:  Fibrillar adhesions; Focal adhesions specifically maturation.

Other adhesion components can be found here.


Tensin is a cytoskeleton scaffolding protein that was named for its ability to form a bridge that maintains tension between the actin filaments and cell-matrix adhesion sites (reviewed in [1]). Tensin contains three actin-binding domains (ABDs) that allows it to form crosslinks along actin filaments; it also prevents actin assembly by capping actin filaments at the barbed end [2, 3]. Tensin has numerous phosphorylation sites and multiple protein interaction domains for both structural components (e.g. paxillin, β-integrin [4]) and signaling molecules (e.g. Src, phosphatidylinositol 3-kinase [PI3K], focal adhesion kinase [FAK]) [5] (reviewed in [6]). Phosphorlyation of tensin corresponds with cell-ECM binding [7] and growth factor stimulation [8] (reviewed in [1]). Tensin forms a C-shaped structure [9] that binds focal adhesion components at both ends [10]. Tensin is also proposed to form a dimer via its carboxy-terminus and this association may be dependent upon its phosphorylation state [9].

 
Figure: Tensin. This schematic diagram illustrates the molecular organization of tensin and provides examples for how tensin is represented in figures throughout this resource. Relevant domains believed to be important for binding to actin and for protein-protein interactions are highlighted (reviewed in [1, 6]). PIP2phosphatidylinositol [4, 5]-bis-phosphate; YP- phosphotyrosine; SH2- Src homology 2.

Protein localization and function

Tensin primarily localizes to sites of cell attachment such as focal adhesions [10, 11], elongated fibrillar structures (aka fibrillar adhesions)[12] and possibly other adhesive junctions [13]. Tensin serves as a link between signal transduction pathways and the actin cytoskeleton by forming a structural platform that regulates the assembly of focal adhesion components, phosphoproteins, and signaling molecules for processes such as cell migration [10, 14] and tissue regeneration [15].
Subpages (1): Figure: Tensin
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tensin_proteins.csv
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Steven Wolf,
Mar 12, 2012 9:15 PM
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tensin_pubmed.csv
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Steven Wolf,
Mar 12, 2012 9:15 PM
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