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CHMP5 is essential for late endosome function and down-regulation of receptor signaling during mouse embryogenesis

Jae-Hyuck Shim1, Changchun Xiao, Matthew S Hayden

  • 1Section of Immunobiology, Ludwig Institute for Cancer Research, Yale University School of Medicine, New Haven, CT 06520, USA.

The Journal of Cell Biology
|March 29, 2006
PubMed

Insights

Charged MVB protein 5 (CHMP5) loss causes embryonic lethality due to defective late endosome function. This CHMP5 protein is crucial for regulating endosome-lysosome trafficking and signal transduction pathways.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Charged MVB protein 5 (CHMP5) is a coiled-coil protein and a member of the ESCRT-III complex.
  • Its specific role in yeast and mammalian cells remains largely uncharacterized.

Purpose of the Study:

  • To investigate the function of CHMP5 in mammalian cells.
  • To elucidate the role of CHMP5 in endosome-MVB pathway and signal transduction.

Main Methods:

  • Gene deletion of CHMP5 in mice (Chmp5-/-).
  • Analysis of cellular phenotypes, including late endosome morphology and function.
  • Assessment of protein degradation and signal transduction pathways.

Main Results:

  • Chmp5-/- mice exhibited early embryonic lethality.
  • Chmp5-/- cells displayed enlarged late endosomal compartments with impaired cargo trafficking to lysosomes.
  • Reduced cellular degradative capacity and accumulation of undigested proteins were observed.
  • Loss of CHMP5 enhanced signal transduction by inhibiting lysosomal degradation of activated receptors.

Conclusions:

  • CHMP5 is essential for mammalian embryonic development.
  • CHMP5 regulates late endosome function downstream of multivesicular body formation.
  • CHMP5 plays a critical role in protein degradation and signal transduction regulation via the endosome-lysosome pathway.

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