Tensin1 and a previously undocumented family member, tensin2, positively regulate cell migration.

Tensin is a focal adhesion molecule that binds to actin filaments and participates in signaling pathways. In this study, we have characterized a previously undocumented tensin family member, tensin2/KIAA 1075. Human tensin2 cDNA encodes a 1,285-aa sequence that shares extensive homology with tensin1 at its amino- and carboxyl-terminal ends, which include the actin-binding domain, the Src homology 2 (SH2) domain, and the phosphotyrosine binding (PTB) domain. Analysis of the genomic structures of tensin1 and tensin2 further confirmed that they represent a single gene family. Examination of tensin2 mRNA distribution revealed that heart, kidney, skeletal muscle, and liver were tissues of high expression. The endogenous and recombinant tensin2 were expressed as a 170-kDa protein in NIH 3T3 cells. The subcellular localization of tensin2 was determined by transfection of green fluorescence protein (GFP)-tensin2 fusion construct. The results indicated that tensin2 is also localized to focal adhesions. Finally, functional analysis of tensin genes has demonstrated that expression of tensin genes is able to promote cell migration on fibronectin, indicating that the tensin family plays a role in regulating cell motility.