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Control of p62 binding to TGN38/41 by phosphorylation.

Authors
  • Zehavi-Feferman, R
  • Burgess, J W
  • Stanley, K K
Type
Published Article
Journal
FEBS Letters
Publisher
Wiley (John Wiley & Sons)
Publication Date
Jul 10, 1995
Volume
368
Issue
1
Pages
122–124
Identifiers
PMID: 7615064
Source
Medline
License
Unknown

Abstract

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.

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