Emerging evidence for kindlin oligomerization and its role in regulating kindlin function

ABSTRACT Integrin-mediated cell–extracellular matrix (ECM) interactions play crucial roles in a broad range of physiological and pathological processes. Kindlins are important positive regulators integrin activation. The FERM-domain-containing kindlin family comprises three members, kindlin-1, kindlin-2 kindlin-3 (also known as FERMT1, FERMT2 FERMT3), which share high sequence similarity (identity >50%), well domain organization, but exhibit diverse tissue-specific expression patterns cellular functions. Given the significance kindlins, analysis their atomic structures has been an attractive field for decades. Recently, its ?-integrin-bound form have obtained, greatly advance our understanding molecular functions that involve kindlins. In particular, emerging evidence indicates oligomerization kindlins might affect binding focal adhesion localization, positively or negatively. this Review, we presented update on recent progress obtaining structures, discuss implication activation based oligomerization, possible regulation process.