The hunt for huntingtin function: interaction partners tell many different stories

Trends Biochem Sci. 2003 Aug;28(8):425-33. doi: 10.1016/S0968-0004(03)00168-3.

Abstract

Huntington's disease (HD) is a neurodegenerative disorder caused by an abnormally elongated polyglutamine (polyQ) tract in the large protein huntingtin (htt). Currently, both the normal function of htt in neurons and the molecular mechanism by which the expanded polyQ sequence in htt causes selective neurodegeneration remain elusive. Research in past years has identified several htt-interacting proteins such as htt-interacting protein 1, Src homology region 3-containing Grb2-like protein 3, protein kinase C and casein kinase substrate in neurons 1, htt-associated protein 1, postsynaptic density-95, FIP-2 (for 14.7K-interacting protein), specificity protein 1 and nuclear receptor co-repressor. These proteins play roles in clathrin-mediated endocytosis, apoptosis, vesicle transport, cell signalling, morphogenesis and transcriptional regulation, suggesting that htt is also involved in these processes.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Apoptosis
  • Axons / metabolism
  • Clathrin / chemistry
  • Dendrites / metabolism
  • Endocytosis
  • Humans
  • Huntingtin Protein
  • Models, Biological
  • Models, Molecular
  • Molecular Sequence Data
  • Nerve Tissue Proteins / chemistry*
  • Nerve Tissue Proteins / physiology*
  • Neurons / metabolism
  • Nuclear Proteins / chemistry*
  • Nuclear Proteins / physiology*
  • Peptides / chemistry
  • Protein Binding
  • Protein Structure, Tertiary
  • Sequence Homology, Amino Acid
  • Signal Transduction
  • Transcription, Genetic

Substances

  • Clathrin
  • HTT protein, human
  • Huntingtin Protein
  • Nerve Tissue Proteins
  • Nuclear Proteins
  • Peptides
  • polyglutamine