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


O'Kelly, Ita, Butler, Margaret H., Zilberberg, Noam and Goldstein, Steve A.N. (2002) Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals. Cell, 111, (4), 577-588. (doi:10.1016/S0092-8674(02)01040-1).

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Description/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.

Item Type: Article
ISSNs: 0092-8674 (print)
Related URLs:
Keywords: proteins, protein transport, research support, nerve tissue, tyrosine 3-monooxygenase, potassium channels, animals, physiology, coatomer protein, amino acid motifs, research
Subjects: Q Science > QK Botany
R Medicine
Q Science > QR Microbiology
Divisions: University Structure - Pre August 2011 > School of Medicine > Developmental Origins of Health and Disease
University Structure - Pre August 2011 > School of Biological Sciences
University Structure - Pre August 2011 > School of Medicine
ePrint ID: 60098
Date Deposited: 08 Sep 2008
Last Modified: 27 Mar 2014 18:42
URI: http://eprints.soton.ac.uk/id/eprint/60098

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