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FEBS Lett. 2017 Jan;591(2):273-281. doi: 10.1002/1873-3468.12532. Epub 2017 Jan 1.

Differential requirement for N-ethylmaleimide-sensitive factor in endosomal trafficking of transferrin receptor from anterograde trafficking of vesicular stomatitis virus glycoprotein G.

Fan J1,2, Zhou X1,2, Wang Y3, Kuang C4, Sun Y1,2, Liu X4, Toomre D5, Xu Y1,2.

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Department of Biomedical Engineering, Key Laboratory of Biomedical Engineering of Ministry of Education, Zhejiang University, Hangzhou, China.
Zhejiang Provincial Key Laboratory of Cardio-Cerebral Vascular Detection Technology and Medicinal Effectiveness Appraisal, Zhejiang University, Hangzhou, China.
Department of Pathology, The First Affiliated Hospital, School of Medicine, Zhejiang University, Hangzhou, China.
Department of Optical Engineering, State Key Laboratory of Modern Optical Instrumentation, Zhejiang University, Hangzhou, China.
Department of Cell Biology, Yale University School of Medicine, New Haven, CT, USA.


N-ethylmaleimide-sensitive fusion factor (NSF) is an ATPase that plays a crucial role in vesicular transport. Here, we examined the effects of NSF knockdown on Golgi structure and different vesicle trafficking pathways in mammalian cells. NSF knockdown caused Golgi fragmentation and abolished transferrin receptor exocytosis, defects that were rescued by RNAi-resistant NSF. Strikingly, NSF deficiency in HeLa cells barely affected cell viability, anterograde trafficking of vesicular stomatitis virus glycoprotein G and transferrin endocytosis. These results confirm the central role of NSF in Golgi structure and reveal differential requirement of NSF for exocytic recycling and constitutive trafficking pathways.


TIRFM ; Golgi; N-ethylmaleimide-sensitive factor; endosome; vesicle trafficking

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