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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

Tensin 1

TNS, Tensin, tensin1
The protein encoded by this gene localizes to focal adhesions, regions of the plasma membrane where the cell attaches to the extracellular matrix. This protein crosslinks actin filaments and contains a Src homology 2 (SH2) domain, which is often found in molecules involved in signal transduction. This protein is a substrate of calpain II. A second transcript from this gene has been described, but its full length nature has not been determined. [provided by RefSeq, Jul 2008] (from NCBI)
Papers on TNS
Effect of five genetic variants associated with lung function on the risk of chronic obstructive lung disease, and their joint effects on lung function.
SpiroMeta Consortium et al., Leicester, United Kingdom. In Am J Respir Crit Care Med, 2011
TNS1 polymorphism associated with COPD risk and lung function decline
Comprehensive analysis of phosphorylation sites in Tensin1 reveals regulation by p38MAPK.
Brautigan et al., Charlottesville, United States. In Mol Cell Proteomics, 2010
data demonstrate that tensin1 is extensively phosphorylated on Ser/Thr residues in cells and phosphorylation by p38 MAPK regulates the specificity of the tensin1 Src homology 2 domain for binding to different proteins
Genome-wide association study identifies five loci associated with lung function.
Tobin et al., Leicester, United Kingdom. In Nat Genet, 2010
Data show expression of TNS1, GSTCD, AGER, HTR4 and THSD4 in lung tissue and indicate potential targets for interventions to alleviate respiratory disease.
Tensin1 requires protein phosphatase-1alpha in addition to RhoGAP DLC-1 to control cell polarization, migration, and invasion.
Brautigan et al., Charlottesville, United States. In J Biol Chem, 2010
Results suggest that PP1alpha bound to tensin1 has effects in reducing migration and invasion that are not mediated through DLC-1, and show the importance of PP1alpha binding to tensin1 for the regulation of cell polarization, migration, and invasion.
[Tensin expression in mesangial cells of human kidney].
Song et al., Harbin, China. In Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi, 2009
The expression of tensin is increased in mesangial cells with stimulating of high concentrations of glucose.
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