Control of p62 binding to TGN38/41 by phosphorylation

FEBS Letters

Burgess, James W.¹  Stanley, Keith K.²  Zehavi-Feferman, Revital² 

[1] 925 Falaise Road, Ottawa, Ont. K2C OM2, Canada;Heart Research Institute, 145 Missenden Road, Camperdown, Sydney NSW 2050, Australia

关键词: Exocytosis;    Membrane traffic;    Targeting signal;    Trans Golgi network;    TGN38 phosphorylation;    CKII;    casein kinase II;    DTSST;    3;    3′-dithiobis-(succinimidylpropionate);    GST;    gluthaione S-transferase;    MPR;    mannos 6-phosphate receptor;    NRK;    normal rat kidney;    PAGE;    polyacrylamide gel electrophoresis;    PKA;    protein kinase A;    PKC;    protein kinase C;    PMA;    phorbol 12-myristate 13-acetate;    PSL;    photostimulatable luminescence;    TGN;    trans-Golgi network;   

DOI  :  10.1016/0014-5793(95)00613-E

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

TGN38/41 cycles between the trans-Golgi network (TGN) and plasma membrane, traversing three sorting compartments: the TGN, plasma membrane and early endosome. The targeting signals responsible for this complex itinerary reside in a short cytoplasmic domain of 33 amino acid residues. We show that phosphorylation of the cytoplasmic domain of TGN38 prevents binding of p62 — a cytoplasmic protein essential for exocytic vesicle formation. Thus the cycle of TGN38/41 traffic, and by implication the pathway of exocytosis, could be controlled by phosphorylation of the TGN38 cytoplasmic domain.

【 授权许可】

Unknown