Differential activity of a variant form of the human Id-1 protein generated by alternative splicing

FEBS Lett. 1998 Oct 2;436(2):169-73. doi: 10.1016/s0014-5793(98)01117-x.

Abstract

Members of the Id family of helix-loop-helix proteins are ubiquitously expressed and dimerize with members of the class A and class B basic helix-loop-helix proteins. Due to the absence of a basic region, Id proteins act as dominant-negative antagonists of basic helix-loop-helix transcription factors, which regulate cell growth and differentiation in diverse cell types. Recent findings suggest that the functions of Id proteins are well regulated at both the transcriptional level and the post-transcriptional level. We show here that the alternative splicing variant of human Id-1 protein possesses a different binding specificity for basic helix-loop-helix transcription factors and is expressed in a cell cycle-dependent manner. Therefore, alternative splicing of Id-1 could provide a post-transcriptional mechanism to regulate Id-1 function.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alternative Splicing*
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cell Line
  • Cloning, Molecular
  • Fibroblasts
  • Genetic Variation*
  • Helix-Loop-Helix Motifs
  • Humans
  • Inhibitor of Differentiation Protein 1
  • Mice
  • Molecular Sequence Data
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Repressor Proteins*
  • Reverse Transcriptase Polymerase Chain Reaction
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Sequence Homology, Nucleic Acid
  • Transcription Factors / chemistry
  • Transcription Factors / genetics*
  • Transcription Factors / metabolism*

Substances

  • ID1 protein, human
  • Idb1 protein, mouse
  • Inhibitor of Differentiation Protein 1
  • Recombinant Proteins
  • Repressor Proteins
  • Transcription Factors