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

被引:31
作者
Kilisch, Markus [1 ]
Lytovchenko, Olga [1 ]
Arakel, Eric C. [1 ]
Bertinetti, Daniela [2 ]
Schwappach, Blanche [1 ,3 ]
机构
[1] Univ Med Gottingen, Dept Mol Biol, Humboldtallee 23, D-37073 Gottingen, Germany
[2] Univ Kassel, Dept Biochem, D-34132 Kassel, Germany
[3] Max Planck Inst Biophys Chem, D-37077 Gottingen, Germany
关键词
14-3-3; protein; Endoplasmic reticulum; Golgi; Membrane trafficking; Phosphorylation; Two-pore-domain K+ channel; COPI; Protein kinase A; TASK-1; POTASSIUM CHANNELS TASK-1; DEPENDENT PROTEIN-KINASE; MEMBRANE-PROTEINS; K+ CHANNELS; TRANSPORT; COATOMER; SUBUNIT; SIGNALS; COPI;
D O I
10.1242/jcs.180182
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
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.
引用
收藏
页码:831 / 842
页数:12
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