Forward transport: 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals
Forward transport: 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals
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 ?-COP to hold channels in ER and a C-terminal “release” site that binds the ubiquitous intracellular regulator 14-3-3? on a nonclassical motif in a phosphorylation-dependent fashion to suppress ?-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 ?-COP and 14-3-3? on adjacent N-terminal sites. Other retained proteins are demonstrated to carry functional 14-3-3? release motifs
proteins, protein transport, research support, nerve tissue, tyrosine 3-monooxygenase, potassium channels, animals, physiology, coatomer protein, amino acid motifs, research
577-588
O'kelly, Ita
e640f28a-42f0-48a6-9ce2-cb5a85d08c66
Butler, Margaret
de1ff527-db81-4f3e-b57a-f37c2dd4d863
Zilberberg, Noam
6a77b1d8-b9f0-46f0-93d3-c402020039e4
Goldstein, Steve A.N.
e957cee2-71ad-4170-a086-5772415f58bc
15 November 2002
O'kelly, Ita
e640f28a-42f0-48a6-9ce2-cb5a85d08c66
Butler, Margaret
de1ff527-db81-4f3e-b57a-f37c2dd4d863
Zilberberg, Noam
6a77b1d8-b9f0-46f0-93d3-c402020039e4
Goldstein, Steve A.N.
e957cee2-71ad-4170-a086-5772415f58bc
O'kelly, Ita, Butler, Margaret, 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), .
(doi:10.1016/S0092-8674(02)01040-1).
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 ?-COP to hold channels in ER and a C-terminal “release” site that binds the ubiquitous intracellular regulator 14-3-3? on a nonclassical motif in a phosphorylation-dependent fashion to suppress ?-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 ?-COP and 14-3-3? on adjacent N-terminal sites. Other retained proteins are demonstrated to carry functional 14-3-3? release motifs
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Published date: 15 November 2002
Keywords:
proteins, protein transport, research support, nerve tissue, tyrosine 3-monooxygenase, potassium channels, animals, physiology, coatomer protein, amino acid motifs, research
Organisations:
Human Genetics
Identifiers
Local EPrints ID: 71946
URI: http://eprints.soton.ac.uk/id/eprint/71946
ISSN: 0092-8674
PURE UUID: 05b09d55-6561-44a4-9c70-59c877741cde
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Date deposited: 13 Jan 2010
Last modified: 13 Mar 2024 20:52
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Contributors
Author:
Ita O'kelly
Author:
Margaret Butler
Author:
Noam Zilberberg
Author:
Steve A.N. Goldstein
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