A vesicle-trafficking protein commandeers Kv channel voltage sensors for voltage-dependent secretion

Growth in plants depends on ion transport for osmotic solute uptake and secretory membrane trafficking to deliver material for wall remodelling and cell expansion. The coordination of these processes lies at the heart of the question, unresolved for more than a century, of how plants regulate cell v...

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Published inNature plants Vol. 1; no. 8; p. 15108
Main Authors Grefen, Christopher, Karnik, Rucha, Larson, Emily, Lefoulon, Cécile, Wang, Yizhou, Waghmare, Sakharam, Zhang, Ben, Hills, Adrian, Blatt, Michael R.
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 03.08.2015
Nature Publishing Group
Subjects
14/19
14/33
631/449/1736
631/449/448/2024
631/449/448/2651
631/80/86/2366
82/111
9/74
Binding
Cell size
Channel gating
Channels
Coordination
Electric potential
Ion transport
Life Sciences
Membrane trafficking
Membranes
Mutation
Plant growth
Plant Sciences
Potassium channels (voltage-gated)
Protein transport
Proteins
Secretion
SNAP receptors
Turgor
Vesicle fusion
Voltage
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Abstract Growth in plants depends on ion transport for osmotic solute uptake and secretory membrane trafficking to deliver material for wall remodelling and cell expansion. The coordination of these processes lies at the heart of the question, unresolved for more than a century, of how plants regulate cell volume and turgor. Here we report that the SNARE protein SYP121 (SYR1/PEN1), which mediates vesicle fusion at the Arabidopsis plasma membrane, binds the voltage sensor domains (VSDs) of K + channels to confer a voltage dependence on secretory traffic in parallel with K + uptake. VSD binding enhances secretion in vivo subject to voltage, and mutations affecting VSD conformation alter binding and secretion in parallel with channel gating, net K + concentration, osmotic content and growth. These results demonstrate a new and unexpected mechanism for secretory control, in which a subset of plant SNAREs commandeer K + channel VSDs to coordinate membrane trafficking with K + uptake for growth. Coordination between vesicle trafficking and osmotic solute uptake is needed for plant growth. It is regulated by the interaction between voltage sensor domains of K + channels and a SNARE protein, conferring a voltage dependence on secretory traffic.
AbstractList Growth in plants depends on ion transport for osmotic solute uptake and secretory membrane trafficking to deliver material for wall remodelling and cell expansion. The coordination of these processes lies at the heart of the question, unresolved for more than a century, of how plants regulate cell volume and turgor. Here we report that the SNARE protein SYP121 (SYR1/PEN1), which mediates vesicle fusion at the Arabidopsis plasma membrane, binds the voltage sensor domains (VSDs) of K+ channels to confer a voltage dependence on secretory traffic in parallel with K+ uptake. VSD binding enhances secretion in vivo subject to voltage, and mutations affecting VSD conformation alter binding and secretion in parallel with channel gating, net K+ concentration, osmotic content and growth. These results demonstrate a new and unexpected mechanism for secretory control, in which a subset of plant SNAREs commandeer K+ channel VSDs to coordinate membrane trafficking with K+ uptake for growth.Coordination between vesicle trafficking and osmotic solute uptake is needed for plant growth. It is regulated by the interaction between voltage sensor domains of K+ channels and a SNARE protein, conferring a voltage dependence on secretory traffic.
Growth in plants depends on ion transport for osmotic solute uptake and secretory membrane trafficking to deliver material for wall remodelling and cell expansion. The coordination of these processes lies at the heart of the question, unresolved for more than a century, of how plants regulate cell volume and turgor. Here we report that the SNARE protein SYP121 (SYR1/PEN1), which mediates vesicle fusion at the Arabidopsis plasma membrane, binds the voltage sensor domains (VSDs) of K(+) channels to confer a voltage dependence on secretory traffic in parallel with K(+) uptake. VSD binding enhances secretion in vivo subject to voltage, and mutations affecting VSD conformation alter binding and secretion in parallel with channel gating, net K(+) concentration, osmotic content and growth. These results demonstrate a new and unexpected mechanism for secretory control, in which a subset of plant SNAREs commandeer K(+) channel VSDs to coordinate membrane trafficking with K(+) uptake for growth.Growth in plants depends on ion transport for osmotic solute uptake and secretory membrane trafficking to deliver material for wall remodelling and cell expansion. The coordination of these processes lies at the heart of the question, unresolved for more than a century, of how plants regulate cell volume and turgor. Here we report that the SNARE protein SYP121 (SYR1/PEN1), which mediates vesicle fusion at the Arabidopsis plasma membrane, binds the voltage sensor domains (VSDs) of K(+) channels to confer a voltage dependence on secretory traffic in parallel with K(+) uptake. VSD binding enhances secretion in vivo subject to voltage, and mutations affecting VSD conformation alter binding and secretion in parallel with channel gating, net K(+) concentration, osmotic content and growth. These results demonstrate a new and unexpected mechanism for secretory control, in which a subset of plant SNAREs commandeer K(+) channel VSDs to coordinate membrane trafficking with K(+) uptake for growth.
Growth in plants depends on ion transport for osmotic solute uptake and secretory membrane trafficking to deliver material for wall remodelling and cell expansion. The coordination of these processes lies at the heart of the question, unresolved for more than a century, of how plants regulate cell volume and turgor. Here we report that the SNARE protein SYP121 (SYR1/PEN1), which mediates vesicle fusion at the Arabidopsis plasma membrane, binds the voltage sensor domains (VSDs) of K + channels to confer a voltage dependence on secretory traffic in parallel with K + uptake. VSD binding enhances secretion in vivo subject to voltage, and mutations affecting VSD conformation alter binding and secretion in parallel with channel gating, net K + concentration, osmotic content and growth. These results demonstrate a new and unexpected mechanism for secretory control, in which a subset of plant SNAREs commandeer K + channel VSDs to coordinate membrane trafficking with K + uptake for growth. Coordination between vesicle trafficking and osmotic solute uptake is needed for plant growth. It is regulated by the interaction between voltage sensor domains of K + channels and a SNARE protein, conferring a voltage dependence on secretory traffic.
Growth in plants depends on ion transport for osmotic solute uptake and secretory membrane trafficking to deliver material for wall remodelling and cell expansion. The coordination of these processes lies at the heart of the question, unresolved for more than a century, of how plants regulate cell volume and turgor. Here we report that the SNARE protein SYP121 (SYR1/PEN1), which mediates vesicle fusion at the Arabidopsis plasma membrane, binds the voltage sensor domains (VSDs) of K(+) channels to confer a voltage dependence on secretory traffic in parallel with K(+) uptake. VSD binding enhances secretion in vivo subject to voltage, and mutations affecting VSD conformation alter binding and secretion in parallel with channel gating, net K(+) concentration, osmotic content and growth. These results demonstrate a new and unexpected mechanism for secretory control, in which a subset of plant SNAREs commandeer K(+) channel VSDs to coordinate membrane trafficking with K(+) uptake for growth.
ArticleNumber 15108
Author Larson, Emily
Blatt, Michael R.
Wang, Yizhou
Hills, Adrian
Waghmare, Sakharam
Zhang, Ben
Grefen, Christopher
Lefoulon, Cécile
Karnik, Rucha
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Snippet Growth in plants depends on ion transport for osmotic solute uptake and secretory membrane trafficking to deliver material for wall remodelling and cell...
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SubjectTerms 14/19
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631/449/1736
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631/449/448/2651
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82/111
9/74
Binding
Cell size
Channel gating
Channels
Coordination
Electric potential
Ion transport
Life Sciences
Membrane trafficking
Membranes
Mutation
Plant growth
Plant Sciences
Potassium channels (voltage-gated)
Protein transport
Proteins
Secretion
SNAP receptors
Turgor
Vesicle fusion
Voltage
Title A vesicle-trafficking protein commandeers Kv channel voltage sensors for voltage-dependent secretion
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