The LIM domain: from the cytoskeleton to the nucleus.
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.
Kadrmas
Julie L
JL
Huntsman Cancer Institute and the Department of Biology, University of Utah, 2000 East, Circle of Hope, Salt Lake City, Utah 84112, USA.
Beckerle
Mary C
MC
D000818:Animals; D015374:Biosensing Techniques; D002467:Cell Nucleus / Q000378:metabolism*; D003545:Cysteine / Q000737:chemistry; D003599:Cytoskeleton / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008954:Models, Biological; D008958:Models, Molecular; D009474:Neurons / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary
D003545:Cysteine