Inhibition of the membrane fusion machinery prevents exit from the TGN and proteolytic processing by furin

FEBS Letters

Kääriäinen, Leevi²  Band, Arja M.¹  Määttä, Juha¹  Kuismanen, Esa¹ 

[1] Department of Biosciences, Division of Biochemistry, Viikki Biocenter, Viikinkaari 5, 00014 University of Helsinki, Helsinki, Finland;Institute of Biotechnology, Viikki Biocenter, Viikinkaari 5, 00014 University of Helsinki, Helsinki, Finland

关键词: Semliki Forest virus;    Furin;    Transport;    Membrane fusion;    Membrane trafficking;    EEA1;    early endosomal autoantigen 1;    GDI;    GDP dissociation inhibitor;    NEM;    N-ethylmaleimide;    NSF;    N-ethylmaleimide-sensitive fusion protein;    SFV;    Semliki Forest virus;    SLO;    streptolysin O;    SNAP;    soluble NSF attachment protein;    TM;    transport medium;    VSV;    vesicular stomatitis virus;   

DOI  :  10.1016/S0014-5793(01)02798-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The Semliki Forest virus (SFV) glycoprotein precursor p62 is processed to the E2 and E3 during the transport from the trans-Golgi network (TGN) to the cell surface. We have studied the regulation of the membrane fusion machinery (Rab/N-ethylmaleimide (NEM)-sensitive fusion protein (NSF)/soluble NSF attachment protein (SNAP)–SNAP receptor) in this processing. Activation of the disassembly of this complex with recombinant NSF stimulated the cleavage of p62 in permeabilized cells. Inactivation of NSF with a mutant α-SNAP(L294A) or NEM treatment inhibited processing of p62. Rab GDP dissociation inhibitor inhibited the cleavage. Inactivation of NSF blocks the transport of SFV glycoproteins and vesicular stomatitis virus G-glycoprotein from the TGN membranes to the cell surface. The results support the conclusion that inhibition of membrane fusion arrests p62 in the TGN and prevents its processing by furin.

【 授权许可】

Unknown