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Gating control and K(+) uptake by the KAT1 K(+) channel leaveraged through membrane anchoring of the trafficking protein SYP121
Vesicle traffic is tightly coordinated with ion transport for plant cell expansion through physical interactions between subsets of vesicle‐trafficking (so‐called SNARE) proteins and plasma membrane Kv channels, including the archetypal inward‐rectifying K(+) channel, KAT1 of Arabidopsis. Ion channe...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6220998/ https://www.ncbi.nlm.nih.gov/pubmed/29940699 http://dx.doi.org/10.1111/pce.13392 |
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author | Lefoulon, Cécile Waghmare, Sakharam Karnik, Rucha Blatt, Michael R. |
author_facet | Lefoulon, Cécile Waghmare, Sakharam Karnik, Rucha Blatt, Michael R. |
author_sort | Lefoulon, Cécile |
collection | PubMed |
description | Vesicle traffic is tightly coordinated with ion transport for plant cell expansion through physical interactions between subsets of vesicle‐trafficking (so‐called SNARE) proteins and plasma membrane Kv channels, including the archetypal inward‐rectifying K(+) channel, KAT1 of Arabidopsis. Ion channels open and close rapidly over milliseconds, whereas vesicle fusion events require many seconds. Binding has been mapped to conserved motifs of both the Kv channels and the SNAREs, but knowledge of the temporal kinetics of their interactions, especially as it might relate to channel gating and its coordination with vesicle fusion remains unclear. Here, we report that the SNARE SYP121 promotes KAT1 gating through a persistent interaction that alters the stability of the channel, both in its open and closed states. We show, too, that SYP121 action on the channel open state requires SNARE anchoring in the plasma membrane. Our findings indicate that SNARE binding confers a conformational bias that encompasses the microscopic kinetics of channel gating, with leverage applied through the SNARE anchor in favour of the open channel. |
format | Online Article Text |
id | pubmed-6220998 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-62209982018-11-15 Gating control and K(+) uptake by the KAT1 K(+) channel leaveraged through membrane anchoring of the trafficking protein SYP121 Lefoulon, Cécile Waghmare, Sakharam Karnik, Rucha Blatt, Michael R. Plant Cell Environ Original Articles Vesicle traffic is tightly coordinated with ion transport for plant cell expansion through physical interactions between subsets of vesicle‐trafficking (so‐called SNARE) proteins and plasma membrane Kv channels, including the archetypal inward‐rectifying K(+) channel, KAT1 of Arabidopsis. Ion channels open and close rapidly over milliseconds, whereas vesicle fusion events require many seconds. Binding has been mapped to conserved motifs of both the Kv channels and the SNAREs, but knowledge of the temporal kinetics of their interactions, especially as it might relate to channel gating and its coordination with vesicle fusion remains unclear. Here, we report that the SNARE SYP121 promotes KAT1 gating through a persistent interaction that alters the stability of the channel, both in its open and closed states. We show, too, that SYP121 action on the channel open state requires SNARE anchoring in the plasma membrane. Our findings indicate that SNARE binding confers a conformational bias that encompasses the microscopic kinetics of channel gating, with leverage applied through the SNARE anchor in favour of the open channel. John Wiley and Sons Inc. 2018-08-01 2018-11 /pmc/articles/PMC6220998/ /pubmed/29940699 http://dx.doi.org/10.1111/pce.13392 Text en © 2018 The Authors Plant, Cell & Environment Published by John Wiley & Sons Ltd This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Original Articles Lefoulon, Cécile Waghmare, Sakharam Karnik, Rucha Blatt, Michael R. Gating control and K(+) uptake by the KAT1 K(+) channel leaveraged through membrane anchoring of the trafficking protein SYP121 |
title | Gating control and K(+) uptake by the KAT1 K(+) channel leaveraged through membrane anchoring of the trafficking protein SYP121
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title_full | Gating control and K(+) uptake by the KAT1 K(+) channel leaveraged through membrane anchoring of the trafficking protein SYP121
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title_fullStr | Gating control and K(+) uptake by the KAT1 K(+) channel leaveraged through membrane anchoring of the trafficking protein SYP121
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title_full_unstemmed | Gating control and K(+) uptake by the KAT1 K(+) channel leaveraged through membrane anchoring of the trafficking protein SYP121
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title_short | Gating control and K(+) uptake by the KAT1 K(+) channel leaveraged through membrane anchoring of the trafficking protein SYP121
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title_sort | gating control and k(+) uptake by the kat1 k(+) channel leaveraged through membrane anchoring of the trafficking protein syp121 |
topic | Original Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6220998/ https://www.ncbi.nlm.nih.gov/pubmed/29940699 http://dx.doi.org/10.1111/pce.13392 |
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