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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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.
|Digital Object Identifier (DOI):||doi:10.1016/S0092-8674(02)01040-1|
|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
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
|Accepted Date and Publication Date:||
|Date Deposited:||08 Sep 2008|
|Last Modified:||06 Aug 2015 02:48|
|RDF:||RDF+N-Triples, RDF+N3, RDF+XML, Browse.|
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