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Vps41, a protein involved in lysosomal trafficking, interacts with caspase-8

Lu Wang1, Xiao Pan, Liangqiang He

  • 1The State Key Laboratory of Pharmaceutical Biotechnology and School of Stomatology, Affiliated Stomatological Hospital, Nanjing University, Nanjing, PR China.

Acta Biochimica Polonica
|November 23, 2012
PubMed

Insights

This study identifies Vacuolar protein sorting 41 (Vps41) as a novel binding partner of caspase-8. Vps41 enhances Fas-induced apoptosis, suggesting a role beyond protein trafficking.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Caspase-8 is a key regulator of apoptosis and cellular development.
  • Vacuolar protein sorting 41 (Vps41) is primarily known for its role in protein trafficking from the Golgi to the vacuole.

Purpose of the Study:

  • To identify novel interacting proteins of caspase-8.
  • To investigate the functional role of Vps41 in apoptosis.

Main Methods:

  • Yeast two-hybrid screening of cDNA libraries.
  • Co-immunoprecipitation (co-IP) assays.
  • Co-localization studies in HEK293T cells.
  • Overexpression studies in A549 human lung adenocarcinoma cells.

Main Results:

  • Identified Vps41 as a caspase-8 interacting protein.
  • Confirmed the interaction between Vps41 and caspase-8 via co-IP and co-localization.
  • Vps41 binds to the p18 subunit of caspase-8.
  • Overexpression of Vps41 promotes Fas-induced apoptosis and increases caspase-3 cleavage.

Conclusions:

  • Vps41 interacts with caspase-8, suggesting a novel role in apoptosis regulation.
  • Vps41 may function beyond its established role in lysosomal trafficking.

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