9.B.87.1.8
Integrin β-1 (ITGB1, FNRB, MDF2, MSK12) of 798 aas and 2 TMSs, N- and C-termini, is a collagen receptor.  Inhibition of endothelial cell migration by thrombospondin-1 type-1 repeats is mediated by beta1 integrins (Short et al. 2005). Integrin beta1 interacts with integrins α1 - 11 to form receptors for fibronectin, laminin, several bacteria and viruses and many other extracellular proteins, and it facilitates sperm-egg fusion (Paul et al. 2015). It forms a tight complex with CD98hc (TC# 8.A.9.2.2) and TrpV4 (TC# 1.A.4.2.5) in focal adhesions where mechanochemical conversion takes place. CD98hc knock down inhibits TRPV4-mediated calcium influx induced by mechanical forces, but not by chemical activators, thus confirming the mechanospecificity of this signaling response. Molecular analysis revealed that forces applied to beta1 integrin must be transmitted from its cytoplasmic C-terminus via the CD98hc cytoplasmic tail to the ankyrin repeat domain of TRPV4 in order to produce ultra-rapid, force-induced, channel activation within the focal adhesion (Potla et al. 2020). A 3-d cryoEM strcuture is available (Cai et al. 2022).