Missense mutation of a conserved residue in UNC-112 (kindlin) eliminates binding to PAT-4 (ILK).

ABSTRACT: C. elegans UNC-112 (kindlin) is required for muscle sarcomere assembly, and is one component of a conserved four-protein complex that associates with the cytoplasmic tail of integrin at the base of integrin adhesion complexes in muscle. The four-protein complex consists of UNC-112 (kindlin), PAT-4 (integrin linked kinase; ILK), PAT-6 (alpha-parvin), and UNC-97 (PINCH). UNC-112 is comprised of 720 amino acid residues and contains FERM and PH domains. The N-terminal half of UNC-112 (1-396 aa) can bind to the C-terminal half of UNC-112 (397-720 aa), and this interaction is inhibited by the association of PAT-4 (ILK) to the N-terminal half of UNC-112. In support of this model, previously, we reported identification of a D382V mutation that results in lack of binding to PAT-4. However, this res

SUBMITTER: Qadota H 

PROVIDER: S-EPMC8449257 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature