A short history of LIM domains (1993-2002): from protein interaction to degradation

Mol Neurobiol. Oct-Dec 2002;26(2-3):269-81. doi: 10.1385/MN:26:2-3:269.

Abstract

The LIM domain is a cysteine-rich zinc-finger motif found in a large family of proteins. In LIM-homeodomain (LIM-hd) transcription factors and LIM-only (LMO) factors, the LIM domains are responsible for key interactions with co-activators, co-repressors, competitors, and other transcription factors, and are therefore of considerable importance for the regulation of associated transcriptional activity. In this review, the authors describe the progressive discoveries of NLI/Ldb/CLIM, LMO and RLIM, and discuss how the field was very recently updated by the finding that LIM-hd transcriptional activity is controlled by regulated degradation of cofactors and LIM-hd themselves.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Eye Proteins / chemistry
  • Eye Proteins / metabolism*
  • Eye Proteins / physiology
  • Homeodomain Proteins / chemistry
  • Homeodomain Proteins / metabolism*
  • Homeodomain Proteins / physiology
  • Humans
  • LIM-Homeodomain Proteins
  • Membrane Proteins
  • Protein Interaction Mapping / methods
  • Transcription Factors

Substances

  • Eye Proteins
  • Homeodomain Proteins
  • LHX1 protein, human
  • LIM-Homeodomain Proteins
  • LIM2 protein, human
  • Membrane Proteins
  • Transcription Factors