The ability of the LIMD1 and TRIP6 LIM domains to bind strained f-actin is critical for their tension dependent localization to adherens junctions and association with the Hippo pathway kinase LATS1.

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Title: The ability of the LIMD1 and TRIP6 LIM domains to bind strained f-actin is critical for their tension dependent localization to adherens junctions and association with the Hippo pathway kinase LATS1.
Authors: Ray S; Department of Biochemistry & Molecular Biotechnology, UMass Chan Medical School, Worcester, Massachusetts, USA., DeSilva C; Department of Biochemistry & Molecular Biotechnology, UMass Chan Medical School, Worcester, Massachusetts, USA., Dasgupta I; Department of Biochemistry & Molecular Biotechnology, UMass Chan Medical School, Worcester, Massachusetts, USA., Mana-Capelli S; Department of Biochemistry & Molecular Biotechnology, UMass Chan Medical School, Worcester, Massachusetts, USA., Cruz-Calderon N; Department of Biochemistry & Molecular Biotechnology, UMass Chan Medical School, Worcester, Massachusetts, USA., McCollum D; Department of Biochemistry & Molecular Biotechnology, UMass Chan Medical School, Worcester, Massachusetts, USA.
Source: Cytoskeleton (Hoboken, N.J.) [Cytoskeleton (Hoboken)] 2024 Sep; Vol. 81 (9-10), pp. 436-447. Date of Electronic Publication: 2024 Mar 01.
Publication Type: Journal Article
Journal Info: Publisher: Wiley-Liss Country of Publication: United States NLM ID: 101523844 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1949-3592 (Electronic) Linking ISSN: 19493592 NLM ISO Abbreviation: Cytoskeleton (Hoboken) Subsets: MEDLINE
Database: MEDLINE Ultimate
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ISSN:1949-3592
DOI:10.1002/cm.21847