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  A dual phosphorylation switch controls 14-3-3-dependent cell surface expression of TASK-1.

Kilisch, M., Lytovchenko, O., Arakel, E. C., Bertinetti, D., & Schwappach, B. (2016). A dual phosphorylation switch controls 14-3-3-dependent cell surface expression of TASK-1. Journal of Cell Science, 129(4), 831-842. doi:10.1242/jcs.180182.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-CCA9-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-CBA6-F
Genre: Journal Article

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 Creators:
Kilisch, M., Author
Lytovchenko, O., Author
Arakel, E. C., Author
Bertinetti, D., Author
Schwappach, B.1, Author              
Affiliations:
1Max Planck Fellow Blanche Schwappach, ou_1548137              

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Free keywords: 14-3-3 protein; Endoplasmic reticulum; Golgi; Membrane trafficking; Phosphorylation; Two-pore-domain K+ channel; COPI; Protein kinase A; TASK-1
 Abstract: The transport of the K+ channels TASK-1 and TASK-3 (also known as KCNK3 and KCNK9, respectively) to the cell surface is controlled by the binding of 14-3-3 proteins to a trafficking control region at the extreme C-terminus of the channels. The current model proposes that phosphorylation-dependent binding of 14-3-3 sterically masks a COPI-binding motif. However, the direct effects of phosphorylation on COPI binding and on the binding parameters of 14-3-3 isoforms are still unknown. We find that phosphorylation of the trafficking control region prevents COPI binding even in the absence of 14-3-3, and we present a quantitative analysis of the binding of all human 14-3-3 isoforms to the trafficking control regions of TASK-1 and TASK-3. Surprisingly, the affinities of 14-3-3 proteins for TASK-1 are two orders of magnitude lower than for TASK-3. Furthermore, we find that phosphorylation of a second serine residue in the C-terminus of TASK-1 inhibits 14-3-3 binding. Thus, phosphorylation of the trafficking control region can stimulate or inhibit transport of TASK-1 to the cell surface depending on the target serine residue. Our findings indicate that control of TASK-1 trafficking by COPI, kinases, phosphatases and 14-3-3 proteins is highly dynamic.

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Language(s): eng - English
 Dates: 2016-02-15
 Publication Status: Published in print
 Pages: -
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 Rev. Method: Peer
 Identifiers: DOI: 10.1242/jcs.180182
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Title: Journal of Cell Science
Source Genre: Journal
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Pages: - Volume / Issue: 129 (4) Sequence Number: - Start / End Page: 831 - 842 Identifier: -