Kindlin-2 is a scaffolding protein that enhances integrin activation mediated by TLN1 and/or TLN2, but activates integrins only weakly by itself. It binds to membranes enriched in phosphoinositides. It also enhances integrin-mediated cell adhesion onto the extracellular matrix and cell spreading; this requires both its ability to interact with integrins and with phospholipid membranes. Kindlin-2 is required for the assembly of focal adhesions and participates in the connection between extracellular matrix adhesion sites and the actin cytoskeleton and also in the orchestration of actin assembly and cell shape modulation. Kindlin-2 recruits FBLIM1 to focal adhesions. It plays a role in the TGFB1 and integrin signaling pathways, and it stabilizes active CTNNB1 and plays a role in the regulation of transcription mediated by CTNNB1 and TCF7L2/TCF4 and in Wnt signaling [taken from the Universal Protein Resource (UniProt) www.uniprot.org/uniprot/Q96AC1].
fermitin family homolog 2 (Drosophila)•
mitogen inducible gene 2 protein•
mitogen-inducible gene 2 protein•
PH domain-containing family C member 1•
pleckstrin homology domain containing, family C (with FERM domain) member 1•
pleckstrin homology domain containing, family C member 1•
pleckstrin homology domain-containing family C member 1•