Tensin-1 (TNS1)

Tensin-1 is a large multidomain scaffolding protein that localizes to focal adhesions, specialized plasma membrane structures where it links the actin cytoskeleton to integrin receptors and supports cell-matrix adhesion[2][3][4][1]. It contains a phosphotyrosine-binding domain that interacts with the cytoplasmic tails of β integrins, and a protein tyrosine phosphatase (PTP) domain that is catalytically inactive in Tensin-1, distinguishing it from enzymatically active PTP family members[2][4]. Tensin-1 participates in organizing actin filaments, modulating signaling pathways, and regulating cellular processes such as migration, polarity, and ECM assembly[1][3][4]. Phase separation properties have recently been described, with Tensin-1 forming membraneless biomolecular condensates during focal adhesion disassembly, highlighting a role in cell cycle-dependent adhesion and signaling dynamics[1]. Dysregulation of Tensin-1 expression or post-translational modification is implicated in lung diseases, tissue remodeling, and cancers, but it is not currently a direct therapeutic target.

Other names

Tensin-1TNS1TNSProtein phosphatase 1 regulatory subunit 155PPP1R155Matrix-remodelling-associated protein 6MXRA6MST091MST122MST127MSTP091MSTP122MSTP127DKFZp586K0617matrix-remodelling associated 6