Differences in self-association between kindlin-2 and kindlin-3 are associated with differential integrin binding.
Ontology highlight
ABSTRACT: The integrin family of transmembrane adhesion receptors coordinates complex signaling networks that control the ability of cells to sense and communicate with the extracellular environment. Kindlin proteins are a central cytoplasmic component of these networks, directly binding integrin cytoplasmic domains and mediating interactions with cytoskeletal and signaling proteins. The physiological importance of kindlins is well established, but how the scaffolding functions of kindlins are regulated at the molecular level is still unclear. Here, using a combination of GFP nanotrap association assays, pulldown and integrin-binding assays, and live-cell imaging, we demonstrate that full-length kindlins can oligomerize (self-associate) in mammalian cells, and we propose that this self-association i
SUBMITTER: Kadry YA
PROVIDER: S-EPMC7415974 | biostudies-literature | 2020 Aug
REPOSITORIES: biostudies-literature
ACCESS DATA