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PLoS One. 2013 Dec 13;8(12):e83324. doi: 10.1371/journal.pone.0083324. eCollection 2013.

Rab39a interacts with phosphatidylinositol 3-kinase and negatively regulates autophagy induced by lipopolysaccharide stimulation in macrophages.

Author information

1
Department of Infectious Diseases, Hamamatsu University School of Medicine, Hamamatsu, Shizuoka, Japan.
2
Department of Health Science, Hamamatsu University School of Medicine, Hamamatsu, Shizuoka, Japan.
3
Department of Infectious Diseases, Hamamatsu University School of Medicine, Hamamatsu, Shizuoka, Japan ; Executive Director, Hamamatsu University School of Medicine, Hamamatsu Hamamatsu, Shizuoka, Japan.

Abstract

Rab39a has pleiotropic functions in phagosome maturation, inflammatory activation and neuritogenesis. Here, we characterized Rab39a function in membrane trafficking of phagocytosis and autophagy induction in macrophages. Rab39a localized to the periphery of LAMP2-positive vesicles and showed the similar kinetics on the phagosome to that of LAMP1. The depletion of Rab39a did not influence the localization of LAMP2 to the phagosome, but it augments the autophagosome formation and LC3 processing by lipopolysaccharide (LPS) stimulation. The augmentation of autophagosome formation in Rab39a-knockdown macrophages was suppressed by Atg5 depletion or an inhibitor for phosphatidylinostol 3-kinase (PI3K). Immunoprecipitation analysis revealed that Rab39a interacts with PI3K and that the amino acid residues from 34(th) to 41(st) in Rab39a were indispensable for this interaction. These results suggest that Rab39a negatively regulates the LPS-induced autophagy in macrophages.

PMID:
24349490
PMCID:
PMC3862771
DOI:
10.1371/journal.pone.0083324
[Indexed for MEDLINE]
Free PMC Article

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