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Tensins are structural adaptor proteins localized at focal adhesions. Tensins can act as mechanosensors and participate in the transduction of biochemical signals from the extracellular matrix to the cytoskeleton, acting as an interface able to alter cell behavior in responses to changes in their surrounding environment. This review aims to provide a concise summary of the main functions of the four known tensins in cell and cancer biology, their homology and recently unveiled signaling mechanisms. We focus specifically on how tensin 4 (TNS4/Cten) may contribute to cancer both as an oncogene supporting metastasis and as tumour suppressor in different types of tissue. A better understanding of the cancer mechanistics involving tensins may provide the rationale for development of specific therapeutic strategies.
This is a preprint submission to PeerJ Preprints.
Figure 1 - Structure of members of the Tensin family and phylogenetic tree
(A) Structure of members of the Tensin family. Tensin-1, Tensin-2 and Tensin-3 contain an ABD (actin binding domain), SH2 (Src homology 2) domain and PTB (phosphotyrosine binding domain). Tensin-2 has a conserved protein kinase C region 1 that is not present in other Tensins. TNS4 has a SH2 domain and PTB domain but lacks the ABD. Among all Tensins, Nuclear localization signal (NLS) and Nuclear export signal (NES) was identified in TNS4. (B) Molecular Phylogenetic analysis of tensins by Maximum Likelihood method