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

Lu Wang, Xiao Pan, Liangqiang He, Rong Zhang, Wei Chen, Jing Zhang, Min Lu, Zi Chun Hua*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

3 Scopus citations


Caspase-8 is a member of the cysteine-aspartic acid protease (caspase) family which plays a central role in apoptosis and development. We screened caspase-8 interacting proteins from mouse T-cell lymphoma and 7.5-day embryo cDNA libraries by yeast two-hybrid system and obtained eleven positive clones, including Vacuolar protein sorting 41 (Vps41), a protein involved in trafficking of proteins from the late Golgi to the vacuole. The interaction of Vps41 with caspase-8 was confirmed by co-immunoprecipitation (co-IP) and co-localization studies in HEK293T cells. Co-IP experiments also showed that Vps41 binds to the p18 subunit of caspase-8 through its WD40 region and RING-finger motif. Further more, we found that over expression of Vps41 promotes Fas-induced apoptosis in A549 human lung adenocarcinoma cells. The cleavage of caspase-3, a caspase-8 downstream effector, was increased when cells were transfected with Vps41-over expressing plasmid. Together, these results suggest a novel interaction of caspase-8 with Vps41 and provide a potential role of Vps41 beyond lysosomal trafficking.

Original languageEnglish (US)
Pages (from-to)37-42
Number of pages6
JournalActa biochimica Polonica
Issue number1
StatePublished - 2013


  • Apoptosis
  • Caspase-8
  • Protein interaction
  • Vps41
  • Yeast two-hybrid

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)


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