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

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Wang L., Pan X., He L., Zhang R., Chen W., Zhang J., Lu M., Hua Z.-C.

2013

vol. 60

issue 1

37-42

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. Furthermore, we found that overexpression 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-overexpressing plasmid. Together, these results suggest a novel interaction of caspase-8 with Vps41 and provide a potential role of Vps41 beyond lysosomal trafficking.

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1 Acta Biochimica Polonica

1 2013

1 Chen W.

1 He L.

1 Hua Z.-C.

1 Lu M.

1 Pan X.

1 Wang L.

1 Zhang J.

1 Zhang R.

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