Accumulation of endogenous LITAF in aggresomes

PLoS One. 2012;7(1):e30003. doi: 10.1371/journal.pone.0030003. Epub 2012 Jan 19.

Abstract

LITAF is a 161 amino acid cellular protein which includes a proline rich N-terminus and a conserved C-terminal domain known as the simple-like domain. Mutations in LITAF have been identified in Charcot-Marie tooth disease, a disease characterized by protein aggregates. Cells transfected with cellular LITAF reveal that LITAF is localized to late endosomes/lysosomes. Here we investigated the intracellular localization of endogenous LITAF. We demonstrated that endogenous LITAF accumulates at a discrete cytoplasmic site in BGMK cells that we identify as the aggresome. To determine the domain within LITAF that is responsible for the localization of LITAF to aggresomes, we created a construct that contained the C-terminal simple-like domain of LITAF and found that this construct also localizes to aggresomes. These data suggest the simple-like domain is responsible for targeting endogenous LITAF to the aggresome.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Line
  • Charcot-Marie-Tooth Disease / metabolism
  • Chlorocebus aethiops
  • DNA-Binding Proteins
  • Endosomal Sorting Complexes Required for Transport / genetics
  • Endosomal Sorting Complexes Required for Transport / metabolism
  • Fluorescent Antibody Technique
  • Humans
  • Mice
  • Multiprotein Complexes / genetics
  • Multiprotein Complexes / metabolism*
  • Mutation
  • Nedd4 Ubiquitin Protein Ligases
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism*
  • Polymerase Chain Reaction
  • Transcription Factors / genetics
  • Transcription Factors / metabolism*
  • Ubiquitin-Protein Ligases / genetics
  • Ubiquitin-Protein Ligases / metabolism

Substances

  • DNA-Binding Proteins
  • Endosomal Sorting Complexes Required for Transport
  • Litaf protein, mouse
  • Multiprotein Complexes
  • Nuclear Proteins
  • Transcription Factors
  • Nedd4 Ubiquitin Protein Ligases
  • Ubiquitin-Protein Ligases