HERC3 binding to and regulation by ubiquitin

FEBS Lett. 2001 Jan 12;488(1-2):74-80. doi: 10.1016/s0014-5793(00)02371-1.

Abstract

Members of the HERC (domain homologous to E6 associated protein carboxy-terminus and RCC1 domain protein) family may function both as guanine nucleotide exchange factors and E3 ubiquitin ligases. Here we identify an unstudied member, HERC3. This protein was recognized by specific antibodies in different cell types. HERC3 was located in the cytosol and in vesicular-like structures containing beta-COP, ARF and Rab5 proteins. Involvement of HERC3 in the ubiquitin system was suggested by its ability to interact with ubiquitin. The conserved cysteine in HECT proteins was not essential for this non-covalent binding. Moreover, HERC3 was a substrate of ubiquitination being degraded by the proteasome. These observations indicate a fine regulation of HERC3 and suggest a role in vesicular traffic and ubiquitin-dependent processes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies
  • Cell Fractionation
  • Cell Line
  • Cytoplasmic Vesicles / chemistry
  • Cytosol / chemistry
  • DNA-Binding Proteins / analysis
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism*
  • Fluorescent Antibody Technique
  • Guanine Nucleotide Exchange Factors / analysis
  • Guanine Nucleotide Exchange Factors / chemistry
  • Guanine Nucleotide Exchange Factors / metabolism
  • Humans
  • Protein Binding
  • Protein Structure, Tertiary
  • Protein Transport
  • Transfection
  • Ubiquitin-Protein Ligases
  • Ubiquitins / metabolism*

Substances

  • Antibodies
  • DNA-Binding Proteins
  • Guanine Nucleotide Exchange Factors
  • Ubiquitins
  • HERC3 protein, human
  • Ubiquitin-Protein Ligases