Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals.

Abstract:

:Proteins with dibasic retention motifs are subject to retrograde transport to endoplasmic reticulum (ER) by COPI-coated vesicles. As forward transport requires escape from ER retention, general release mechanisms have been expected. Here, KCNK3 potassium channels are shown to bear two cytoplasmic trafficking motifs: an N-terminal dibasic site that binds beta-COP to hold channels in ER and a C-terminal "release" site that binds the ubiquitous intracellular regulator 14-3-3beta on a nonclassical motif in a phosphorylation-dependent fashion to suppress beta-COP binding and allow forward transport. The strategy appears to be common. The major histocompatibility antigen class II-associated invariant chain Iip35 exhibits dibasic retention, carries a release motif, and shows mutually exclusive binding of beta-COP and 14-3-3beta on adjacent N-terminal sites. Other retained proteins are demonstrated to carry functional 14-3-3beta release motifs.

journal_name

Cell

journal_title

Cell

authors

O'Kelly I,Butler MH,Zilberberg N,Goldstein SA

doi

10.1016/s0092-8674(02)01040-1

subject

Has Abstract

pub_date

2002-11-15 00:00:00

pages

577-88

issue

4

eissn

0092-8674

issn

1097-4172

pii

S0092867402010401

journal_volume

111

pub_type

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