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Control of p62 binding to TGN38/41 by phosphorylation
[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.

[发布日期]  [发布机构] 
[效力级别]  [学科分类] 生物化学/生物物理
[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 [时效性] 
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