The three KINDLINs are a novel family of focal adhesion proteins, localizing to integrin adhesion sites. The KINDLIN proteins are composed of a centrally located FERM domain interrupted by a pleckstrin homology (PH) domain. KINDLIN1 and KINDLIN2 have been shown to play an essential role in integrin-mediated adhesion and spreading. In contrast to the widely expressed KINDLIN1 and KINDLIN2, KINDLIN3 is restricted to hematopoietic cells and is particularly abundant in megakaryocytes and platelets. Several reports describe a transcriptional misregulation of KINDLINs in various types of cancer. A recent study demonstrates that KINDLIN3 is essential for platelet integrin activation and subsequent integrin outside-in signaling, suggesting it may serve as a potential target for the design of therapeutics aimed at specifically disrupting integrin activation in platelets and leukocytes.
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