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Forward transport of K2p3.1: mediation by 14-3-3 and COPI, modulation by p111

Forward transport of K2p3.1: mediation by 14-3-3 and COPI, modulation by p111
Forward transport of K2p3.1: mediation by 14-3-3 and COPI, modulation by p111
Surface expression of the K(2P)3.1 two-pore domain potassium channel is regulated by phosphorylation-dependent binding of 14-3-3, leading to suppression of coatomer coat protein I (COPI)-mediated retention in endoplasmic reticulum (ER). Here, we investigate the nature of the macromolecular regulatory complexes that mediate forward and retrograde transport. We demonstrate that (i) the channel employs two separate but interacting COPI binding sites on the N- and C-termini; (ii) disrupting COPI binding to either site interferes with the ER retention; (iii) p11 and 14-3-3 do not interact on their own; (iv) p11 binding to the C-terminal retention motif is dependent on 14-3-3; and (v) p11 is coexpressed in only a subset of tissues with K(2P)3.1, while 14-3-3 expression is ubiquitous. We conclude that K(2P)3.1 forward transport requires 14-3-3 suppression of COPI binding, whereas p11 serves a modulatory role.
14-3-3, annexin, background, COPI retention, leak, p11, potassium channel, resting potential, TASK-1
1398-9219
72-78
O'Kelly, Ita
e640f28a-42f0-48a6-9ce2-cb5a85d08c66
Goldstein, Steve A.N.
e957cee2-71ad-4170-a086-5772415f58bc
O'Kelly, Ita
e640f28a-42f0-48a6-9ce2-cb5a85d08c66
Goldstein, Steve A.N.
e957cee2-71ad-4170-a086-5772415f58bc

O'Kelly, Ita and Goldstein, Steve A.N. (2008) Forward transport of K2p3.1: mediation by 14-3-3 and COPI, modulation by p111. Traffic, 9 (1), 72-78. (doi:10.1111/j.1600-0854.2007.00663.x).

Record type: Article

Abstract

Surface expression of the K(2P)3.1 two-pore domain potassium channel is regulated by phosphorylation-dependent binding of 14-3-3, leading to suppression of coatomer coat protein I (COPI)-mediated retention in endoplasmic reticulum (ER). Here, we investigate the nature of the macromolecular regulatory complexes that mediate forward and retrograde transport. We demonstrate that (i) the channel employs two separate but interacting COPI binding sites on the N- and C-termini; (ii) disrupting COPI binding to either site interferes with the ER retention; (iii) p11 and 14-3-3 do not interact on their own; (iv) p11 binding to the C-terminal retention motif is dependent on 14-3-3; and (v) p11 is coexpressed in only a subset of tissues with K(2P)3.1, while 14-3-3 expression is ubiquitous. We conclude that K(2P)3.1 forward transport requires 14-3-3 suppression of COPI binding, whereas p11 serves a modulatory role.

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More information

e-pub ahead of print date: 1 October 2007
Published date: January 2008
Keywords: 14-3-3, annexin, background, COPI retention, leak, p11, potassium channel, resting potential, TASK-1
Organisations: Human Development & Health, Medicine

Identifiers

Local EPrints ID: 60100
URI: http://eprints.soton.ac.uk/id/eprint/60100
ISSN: 1398-9219
PURE UUID: ac940e3a-d00c-42e6-b522-d66f5206d059

Catalogue record

Date deposited: 24 Nov 2008
Last modified: 15 Mar 2024 11:19

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Contributors

Author: Ita O'Kelly
Author: Steve A.N. Goldstein

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