The C-terminus of MIP-T3 protein is required for ubiquitin-proteasome-mediated degradation in human cells

FEBS Lett. 2011 May 6;585(9):1350-6. doi: 10.1016/j.febslet.2011.04.015. Epub 2011 Apr 15.

Abstract

The intraflagellar transport (IFT) complex is essential for the formation and functional maintenance of eukaryotic cilia which play a vital role in development and tissue homeostasis. However, the biochemical characteristics and precise functions of IFT proteins remain unknown. Here, we report that MIP-T3, a human microtubule-interacting protein recently identified as a novel conserved component of the IFT complex, is an easily degradable protein in human cell lines. Protein degradation is mediated by the ubiquitin-proteasome system, and the C-terminus is required for ubiquitination and proteasome-mediated degradation of MIP-T3 protein. This study provides the first evidence for regulation of IFT protein stability.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Blotting, Western
  • Cell Line, Tumor
  • Green Fluorescent Proteins / genetics
  • Green Fluorescent Proteins / metabolism
  • HEK293 Cells
  • HeLa Cells
  • Humans
  • Microscopy, Fluorescence
  • Microtubule-Associated Proteins / genetics
  • Microtubule-Associated Proteins / metabolism*
  • Proteasome Endopeptidase Complex / metabolism*
  • Reverse Transcriptase Polymerase Chain Reaction
  • Signal Transduction
  • Ubiquitin / metabolism*

Substances

  • Microtubule-Associated Proteins
  • TRAF3IP1 protein, human
  • Ubiquitin
  • Green Fluorescent Proteins
  • Proteasome Endopeptidase Complex