ArticleMolecular biology of the cell2014
Cooperative endocytosis of the endosomal SNARE protein syntaxin-8 and the potassium channel TASK-1.
Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 30 citations in OpenAlex.
- A versatile functional interaction between electrically silent KCellular and molecular life sciences : CMLS · 2024Article
- Monocytic Differentiation of Human Acute Myeloid Leukemia Cells: A Proteomic and Phosphoproteomic Comparison of FAB-M4/M5 Patients with and without Nucleophosmin 1 Mutations.International journal of molecular sciences · 2024Article
- Analysis of the SNARE Stx8 recycling reveals that the retromer-sorting motif has undergone evolutionary divergence.PLoS genetics · 2021Article
- Pressure-dependent modulation of inward-rectifying KAmerican journal of physiology. Cell physiology · 2019Article
- The VAMP-associated protein VAPB is required for cardiac and neuronal pacemaker channel function.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018Article
- Monoubiquitination of syntaxin 3 leads to retrieval from the basolateral plasma membrane and facilitates cargo recruitment to exosomes.Molecular biology of the cell · 2017Article
- Heterodimerization of two pore domain K+ channel TASK1 and TALK2 in living heterologous expression systems.PloS one · 2017Article
- The family of K2P channels: salient structural and functional properties.The Journal of physiology · 2015Review
- The role of protein-protein interactions in the intracellular traffic of the potassium channels TASK-1 and TASK-3.Pflugers Archiv : European journal of physiology · 2015Review
- Much more than a leak: structure and function of K₂p-channels.Pflugers Archiv : European journal of physiology · 2015Review
- Endocytosis as a mode to regulate functional expression of two-pore domain potassium (K₂p) channels.Pflugers Archiv : European journal of physiology · 2015Review
- Role of K₂p channels in stimulus-secretion coupling.Pflugers Archiv : European journal of physiology · 2015Review
- RNA editing in the central cavity as a mechanism to regulate surface expression of the voltage-gated potassium channel Kv1.1.The Journal of biological chemistry · 2014Article
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11 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The endosomal SNARE protein syntaxin-8 interacts with the acid-sensitive potassium channel TASK-1. The functional relevance of this interaction was studied by heterologous expression of these proteins (and mutants thereof) in Xenopus oocytes and in mammalian cell lines. Coexpression of syntaxin-8 caused a fourfold reduction in TASK-1 current, a corresponding reduction in the expression of TASK-1 at the cell surface, and a marked increase in the rate of endocytosis of the channel. TASK-1 and syntaxin-8 colocalized in the early endosomal compartment, as indicated by the endosomal markers 2xFYVE and rab5. The stimulatory effect of the SNARE protein on the endocytosis of the channel was abolished when both an endocytosis signal in TASK-1 and an endocytosis signal in syntaxin-8 were mutated. A syntaxin-8 mutant that cannot assemble with other SNARE proteins had virtually the same effect as wild-type syntaxin-8. Total internal reflection fluorescence microscopy showed formation and endocytosis of vesicles containing fluorescence-tagged clathrin, TASK-1, and/or syntaxin-8. Our results suggest that the unassembled form of syntaxin-8 and the potassium channel TASK-1 are internalized via clathrin-mediated endocytosis in a cooperative manner. This implies that syntaxin-8 regulates the endocytosis of TASK-1. Our study supports the idea that endosomal SNARE proteins can have functions unrelated to membrane fusion.
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