Overexpression of wild-type and mutant mucolipin proteins in mammalian cells: Effects on the late endocytic compartment organization

M. Manzoni, E. Monti, R. Bresciani, A. Bozzato, S. Barlati, M. T. Bassi, G. Borsani

Research output: Contribution to journalArticle

Abstract

Mucolipin-1 is a 65-kDa membrane protein encoded by the MCOLN1 gene, which is mutated in patients with mucolipidosis type IV (MLIV), a rare neurodegenerative lysosomal storage disorder. We studied the subcellular localization of wild-type and three different mutant forms (T232P, F408del and F465L) of mucolipin by expressing Myc-tagged proteins in HeLa cells. The overexpressed wild-type mucolipin colocalizes to late endocytic structures and induces an aberrant distribution of these compartments. F408del and F465L MLIV mutant proteins show a distribution similar to the wild-type protein, whereas T232P is retained in the endoplasmic reticulum. Among the mutants, only F408del induces a redistribution of the late endocytic compartment. These findings suggest that the overexpression of the mucolipin cation channel influences the dynamic equilibrium of late endocytic compartments.

Original languageEnglish
Pages (from-to)219-224
Number of pages6
JournalFEBS Letters
Volume567
Issue number2-3
DOIs
Publication statusPublished - Jun 4 2004

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Keywords

  • AJ, Ashkenazi Jews
  • Lysosome
  • MCOLN1, mucolipin-1 gene
  • MLIV, mucolipidosis type IV
  • MLN1, mucolipin-1 protein
  • MLN2, mucolipin 2 protein
  • MLN3, mucolipin 3 protein
  • Mucolipidosis type IV
  • Mucolipin
  • PC2, polycystin-2
  • TRP, transient receptor potential

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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