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Gating control and K + uptake by the KAT1 K + channel leaveraged through membrane anchoring of the trafficking protein SYP121
Author(s) -
Lefoulon Cécile,
Waghmare Sakharam,
Karnik Rucha,
Blatt Michael R.
Publication year - 2018
Publication title -
plant, cell and environment
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.646
H-Index - 200
eISSN - 1365-3040
pISSN - 0140-7791
DOI - 10.1111/pce.13392
Subject(s) - gating , vesicle , biophysics , chemistry , ion channel , exocytosis , membrane , microbiology and biotechnology , biology , biochemistry , receptor
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.