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Updated: May 12, 2026

Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner
Published on: December 10, 2015
The LIM domain: from the cytoskeleton to the nucleus
Julie L Kadrmas1, Mary C Beckerle
1Huntsman Cancer Institute and the Department of Biology, University of Utah, 2000 East, Circle of Hope, Salt Lake City, Utah 84112, USA.
Abstract:
First described 15 years ago as a cysteine-rich sequence that was common to a small group of homeodomain transcription factors, the LIM domain is now recognized as a tandem zinc-finger structure that functions as a modular protein-binding interface. LIM domains are present in many proteins that have diverse cellular roles as regulators of gene expression, cytoarchitecture, cell adhesion, cell motility and signal transduction. An emerging theme is that LIM proteins might function as biosensors that mediate communication between the cytosolic and the nuclear compartments.
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