Role of LIM domains in mediating signaling protein interactions.
LIM domains are double zinc-finger motifs that mediate protein interactions between transcription factors, cytoskeletal and signaling proteins. This review outlines the protein interactions mediated by LIM domains with signaling proteins including tyrosine and serine/threonine kinases and phosphatases.
Brown
S
S
Department of Biochemistry and Molecular Biology, Monash University, Melbourne, Australia. Susan.brown@med.monash.edu.au
Coghill
I D
ID
McGrath
M J
MJ
Robinson
P A
PA
D000199:Actins / Q000378:metabolism; D016384:Consensus Sequence; D003598:Cytoskeletal Proteins / Q000737:chemistry* / Q000378:metabolism*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism; D011493:Protein Kinase C / Q000378:metabolism; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D017434:Protein Structure, Tertiary; D011505:Protein-Tyrosine Kinases / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D016335:Zinc Fingers
D000199:Actins; D003598:Cytoskeletal Proteins; D014157:Transcription Factors; D011505:Protein-Tyrosine Kinases; D017346:Protein Serine-Threonine Kinases; D011493:Protein Kinase C; D010744:Phosphoric Monoester Hydrolases