Clustering of the K⁺ channel GORK of Arabidopsis parallels its gating by extracellular K
GORK is the only outward‐rectifying Kv‐like K⁺ channel expressed in guard cells. Its activity is tightly regulated to facilitate K⁺ efflux for stomatal closure and is elevated in ABA in parallel with suppression of the activity of the inward‐rectifying K⁺ channel KAT1. Whereas the population of KAT1...
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| Published in | The Plant journal : for cell and molecular biology Vol. 78; no. 2; pp. 203 - 214 |
|---|---|
| Main Authors | , , , |
| Format | Journal Article |
| Language | English |
| Published |
England
Blackwell Science
01.04.2014
Blackwell Publishing Ltd BlackWell Publishing Ltd |
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| Abstract | GORK is the only outward‐rectifying Kv‐like K⁺ channel expressed in guard cells. Its activity is tightly regulated to facilitate K⁺ efflux for stomatal closure and is elevated in ABA in parallel with suppression of the activity of the inward‐rectifying K⁺ channel KAT1. Whereas the population of KAT1 is subject to regulated traffic to and from the plasma membrane, nothing is known about GORK, its distribution and traffic in vivo. We have used transformations with fluorescently‐tagged GORK to explore its characteristics in tobacco epidermis and Arabidopsis guard cells. These studies showed that GORK assembles in puncta that reversibly dissociated as a function of the external K⁺ concentration. Puncta dissociation parallelled the gating dependence of GORK, the speed of response consistent with the rapidity of channel gating response to changes in the external ionic conditions. Dissociation was also suppressed by the K⁺ channel blocker Ba²⁺. By contrast, confocal and protein biochemical analysis failed to uncover substantial exo‐ and endocytotic traffic of the channel. Gating of GORK is displaced to more positive voltages with external K⁺, a characteristic that ensures the channel facilitates only K⁺ efflux regardless of the external cation concentration. GORK conductance is also enhanced by external K⁺ above 1 mm. We suggest that GORK clustering in puncta is related to its gating and conductance, and reflects associated conformational changes and (de)stabilisation of the channel protein, possibly as a platform for transmission and coordination of channel gating in response to external K⁺. |
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| AbstractList | Summary GORK is the only outward-rectifying Kv-like K+ channel expressed in guard cells. Its activity is tightly regulated to facilitate K+ efflux for stomatal closure and is elevated in ABA in parallel with suppression of the activity of the inward-rectifying K+ channel KAT1. Whereas the population of KAT1 is subject to regulated traffic to and from the plasma membrane, nothing is known about GORK, its distribution and traffic in vivo. We have used transformations with fluorescently-tagged GORK to explore its characteristics in tobacco epidermis and Arabidopsis guard cells. These studies showed that GORK assembles in puncta that reversibly dissociated as a function of the external K+ concentration. Puncta dissociation parallelled the gating dependence of GORK, the speed of response consistent with the rapidity of channel gating response to changes in the external ionic conditions. Dissociation was also suppressed by the K+ channel blocker Ba2+. By contrast, confocal and protein biochemical analysis failed to uncover substantial exo- and endocytotic traffic of the channel. Gating of GORK is displaced to more positive voltages with external K+, a characteristic that ensures the channel facilitates only K+ efflux regardless of the external cation concentration. GORK conductance is also enhanced by external K+ above 1 mm. We suggest that GORK clustering in puncta is related to its gating and conductance, and reflects associated conformational changes and (de)stabilisation of the channel protein, possibly as a platform for transmission and coordination of channel gating in response to external K+. [PUBLICATION ABSTRACT] Summary GORK is the only outward‐rectifying Kv‐like K+ channel expressed in guard cells. Its activity is tightly regulated to facilitate K+ efflux for stomatal closure and is elevated in ABA in parallel with suppression of the activity of the inward‐rectifying K+ channel KAT1. Whereas the population of KAT1 is subject to regulated traffic to and from the plasma membrane, nothing is known about GORK, its distribution and traffic in vivo. We have used transformations with fluorescently‐tagged GORK to explore its characteristics in tobacco epidermis and Arabidopsis guard cells. These studies showed that GORK assembles in puncta that reversibly dissociated as a function of the external K+ concentration. Puncta dissociation parallelled the gating dependence of GORK, the speed of response consistent with the rapidity of channel gating response to changes in the external ionic conditions. Dissociation was also suppressed by the K+ channel blocker Ba2+. By contrast, confocal and protein biochemical analysis failed to uncover substantial exo‐ and endocytotic traffic of the channel. Gating of GORK is displaced to more positive voltages with external K+, a characteristic that ensures the channel facilitates only K+ efflux regardless of the external cation concentration. GORK conductance is also enhanced by external K+ above 1 mm. We suggest that GORK clustering in puncta is related to its gating and conductance, and reflects associated conformational changes and (de)stabilisation of the channel protein, possibly as a platform for transmission and coordination of channel gating in response to external K+. GORK is the only outward-rectifying Kv-like K(+) channel expressed in guard cells. Its activity is tightly regulated to facilitate K(+) efflux for stomatal closure and is elevated in ABA in parallel with suppression of the activity of the inward-rectifying K(+) channel KAT1. Whereas the population of KAT1 is subject to regulated traffic to and from the plasma membrane, nothing is known about GORK, its distribution and traffic in vivo. We have used transformations with fluorescently-tagged GORK to explore its characteristics in tobacco epidermis and Arabidopsis guard cells. These studies showed that GORK assembles in puncta that reversibly dissociated as a function of the external K(+) concentration. Puncta dissociation parallelled the gating dependence of GORK, the speed of response consistent with the rapidity of channel gating response to changes in the external ionic conditions. Dissociation was also suppressed by the K(+) channel blocker Ba(2+) . By contrast, confocal and protein biochemical analysis failed to uncover substantial exo- and endocytotic traffic of the channel. Gating of GORK is displaced to more positive voltages with external K(+) , a characteristic that ensures the channel facilitates only K(+) efflux regardless of the external cation concentration. GORK conductance is also enhanced by external K(+) above 1 mm. We suggest that GORK clustering in puncta is related to its gating and conductance, and reflects associated conformational changes and (de)stabilisation of the channel protein, possibly as a platform for transmission and coordination of channel gating in response to external K(+) .GORK is the only outward-rectifying Kv-like K(+) channel expressed in guard cells. Its activity is tightly regulated to facilitate K(+) efflux for stomatal closure and is elevated in ABA in parallel with suppression of the activity of the inward-rectifying K(+) channel KAT1. Whereas the population of KAT1 is subject to regulated traffic to and from the plasma membrane, nothing is known about GORK, its distribution and traffic in vivo. We have used transformations with fluorescently-tagged GORK to explore its characteristics in tobacco epidermis and Arabidopsis guard cells. These studies showed that GORK assembles in puncta that reversibly dissociated as a function of the external K(+) concentration. Puncta dissociation parallelled the gating dependence of GORK, the speed of response consistent with the rapidity of channel gating response to changes in the external ionic conditions. Dissociation was also suppressed by the K(+) channel blocker Ba(2+) . By contrast, confocal and protein biochemical analysis failed to uncover substantial exo- and endocytotic traffic of the channel. Gating of GORK is displaced to more positive voltages with external K(+) , a characteristic that ensures the channel facilitates only K(+) efflux regardless of the external cation concentration. GORK conductance is also enhanced by external K(+) above 1 mm. We suggest that GORK clustering in puncta is related to its gating and conductance, and reflects associated conformational changes and (de)stabilisation of the channel protein, possibly as a platform for transmission and coordination of channel gating in response to external K(+) . GORK is the only outward‐rectifying Kv‐like K⁺channel expressed in guard cells. Its activity is tightly regulated to facilitate K⁺efflux for stomatal closure and is elevated in ABA in parallel with suppression of the activity of the inward‐rectifying K⁺channel KAT1. Whereas the population of KAT1 is subject to regulated traffic to and from the plasma membrane, nothing is known about GORK, its distribution and traffic in vivo. We have used transformations with fluorescently‐tagged GORK to explore its characteristics in tobacco epidermis and Arabidopsis guard cells. These studies showed that GORK assembles in puncta that reversibly dissociated as a function of the external K⁺concentration. Puncta dissociation parallelled the gating dependence of GORK, the speed of response consistent with the rapidity of channel gating response to changes in the external ionic conditions. Dissociation was also suppressed by the K⁺channel blocker Ba²⁺. By contrast, confocal and protein biochemical analysis failed to uncover substantial exo‐ and endocytotic traffic of the channel. Gating of GORK is displaced to more positive voltages with external K⁺, a characteristic that ensures the channel facilitates only K⁺efflux regardless of the external cation concentration. GORK conductance is also enhanced by external K⁺above 1 mm. We suggest that GORK clustering in puncta is related to its gating and conductance, and reflects associated conformational changes and (de)stabilisation of the channel protein, possibly as a platform for transmission and coordination of channel gating in response to external K⁺. GORK is the only outward-rectifying Kv-like K + channel expressed in guard cells. Its activity is tightly regulated to facilitate K + efflux for stomatal closure and is elevated in ABA in parallel with suppression of the activity of the inward-rectifying K + channel KAT1. Whereas the population of KAT1 is subject to regulated traffic to and from the plasma membrane, nothing is known about GORK, its distribution and traffic in vivo . We have used transformations with fluorescently-tagged GORK to explore its characteristics in tobacco epidermis and Arabidopsis guard cells. These studies showed that GORK assembles in puncta that reversibly dissociated as a function of the external K + concentration. Puncta dissociation parallelled the gating dependence of GORK, the speed of response consistent with the rapidity of channel gating response to changes in the external ionic conditions. Dissociation was also suppressed by the K + channel blocker Ba 2+ . By contrast, confocal and protein biochemical analysis failed to uncover substantial exo- and endocytotic traffic of the channel. Gating of GORK is displaced to more positive voltages with external K + , a characteristic that ensures the channel facilitates only K + efflux regardless of the external cation concentration. GORK conductance is also enhanced by external K + above 1 m m . We suggest that GORK clustering in puncta is related to its gating and conductance, and reflects associated conformational changes and (de)stabilisation of the channel protein, possibly as a platform for transmission and coordination of channel gating in response to external K + . GORK is the only outward‐rectifying Kv‐like K⁺ channel expressed in guard cells. Its activity is tightly regulated to facilitate K⁺ efflux for stomatal closure and is elevated in ABA in parallel with suppression of the activity of the inward‐rectifying K⁺ channel KAT1. Whereas the population of KAT1 is subject to regulated traffic to and from the plasma membrane, nothing is known about GORK, its distribution and traffic in vivo. We have used transformations with fluorescently‐tagged GORK to explore its characteristics in tobacco epidermis and Arabidopsis guard cells. These studies showed that GORK assembles in puncta that reversibly dissociated as a function of the external K⁺ concentration. Puncta dissociation parallelled the gating dependence of GORK, the speed of response consistent with the rapidity of channel gating response to changes in the external ionic conditions. Dissociation was also suppressed by the K⁺ channel blocker Ba²⁺. By contrast, confocal and protein biochemical analysis failed to uncover substantial exo‐ and endocytotic traffic of the channel. Gating of GORK is displaced to more positive voltages with external K⁺, a characteristic that ensures the channel facilitates only K⁺ efflux regardless of the external cation concentration. GORK conductance is also enhanced by external K⁺ above 1 mm. We suggest that GORK clustering in puncta is related to its gating and conductance, and reflects associated conformational changes and (de)stabilisation of the channel protein, possibly as a platform for transmission and coordination of channel gating in response to external K⁺. GORK is the only outward-rectifying Kv-like K(+) channel expressed in guard cells. Its activity is tightly regulated to facilitate K(+) efflux for stomatal closure and is elevated in ABA in parallel with suppression of the activity of the inward-rectifying K(+) channel KAT1. Whereas the population of KAT1 is subject to regulated traffic to and from the plasma membrane, nothing is known about GORK, its distribution and traffic in vivo. We have used transformations with fluorescently-tagged GORK to explore its characteristics in tobacco epidermis and Arabidopsis guard cells. These studies showed that GORK assembles in puncta that reversibly dissociated as a function of the external K(+) concentration. Puncta dissociation parallelled the gating dependence of GORK, the speed of response consistent with the rapidity of channel gating response to changes in the external ionic conditions. Dissociation was also suppressed by the K(+) channel blocker Ba(2+) . By contrast, confocal and protein biochemical analysis failed to uncover substantial exo- and endocytotic traffic of the channel. Gating of GORK is displaced to more positive voltages with external K(+) , a characteristic that ensures the channel facilitates only K(+) efflux regardless of the external cation concentration. GORK conductance is also enhanced by external K(+) above 1 mm. We suggest that GORK clustering in puncta is related to its gating and conductance, and reflects associated conformational changes and (de)stabilisation of the channel protein, possibly as a platform for transmission and coordination of channel gating in response to external K(+) . |
| Author | Eisenach, Cornelia Hillert, Ellin‐Kristina Papanatsiou, Maria Blatt, Michael R |
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| Copyright | 2014 The Authors published by Society for Experimental Biology and John Wiley & Sons Ltd. 2014 The Authors The Plant Journal © 2014 John Wiley & Sons Ltd. Copyright © 2014 John Wiley & Sons Ltd and the Society for Experimental Biology 2014 The Authors published by Society for Experimental Biology and John Wiley & Sons Ltd. 2014 |
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| Keywords | Arabidopsis GORK K+ channel - outward-rectifying confocal microscopy plasma membrane K+ concentration - extracellular channel gating - K+-dependent membrane vesicle traffic |
| Language | English |
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| References | 1997; 158 2002; 14 2011; 439 2013; 25 2010; 15 1990; 346 2010; 107 2011; 62 2007; 581 1992; 126 2012; 160 1988; 102 1999; 283 1990; 180 1992; 99 2009; 479 2010; 61 1998; 16 2009; 14 1991; 185 1998; 17 2000; 16 2004; 136 2000; 124 2001 1980; 30 1999; 19 2005; 102 2004; 39 2004; 37 2005; 226 1989; 264 2000; 97 2000; 486 2012; 69 1998; 95 2012; 23 2001; 213 2007; 17 2010; 33 1995; 92 2009; 21 2000; 115 1993; 44 2006; 7 2006; 393 2005; 41 2011; 30 2007 2006; 18 1993; 90 2013; 142 1991; 138 2007; 12 1999 1997; 202 1997; 203 1998; 39 1990; 116 1963; 11 1990; 114 1997; 405 2006; 46 2010a; 22 1993; 191 2010b; 64 2007; 86 2003; 301 2012; 7 1994; 5 2003; 100 2012; 8 |
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| Snippet | GORK is the only outward‐rectifying Kv‐like K⁺ channel expressed in guard cells. Its activity is tightly regulated to facilitate K⁺ efflux for stomatal closure... Summary GORK is the only outward‐rectifying Kv‐like K+ channel expressed in guard cells. Its activity is tightly regulated to facilitate K+ efflux for stomatal... GORK is the only outward-rectifying Kv-like K(+) channel expressed in guard cells. Its activity is tightly regulated to facilitate K(+) efflux for stomatal... Summary GORK is the only outward-rectifying Kv-like K+ channel expressed in guard cells. Its activity is tightly regulated to facilitate K+ efflux for stomatal... GORK is the only outward‐rectifying Kv‐like K⁺channel expressed in guard cells. Its activity is tightly regulated to facilitate K⁺efflux for stomatal closure... GORK is the only outward-rectifying Kv-like K + channel expressed in guard cells. Its activity is tightly regulated to facilitate K + efflux for stomatal... |
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| SubjectTerms | abscisic acid Arabidopsis Arabidopsis - metabolism Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Arabidopsis Proteins - physiology barium Biochemical analysis Biochemistry Biological Transport Botany Cellular biology channel gating – K+‐dependent confocal microscopy dissociation Epidermis GORK K+ channel – outward‐rectifying guard cells K+ concentration – extracellular membrane vesicle traffic Original plasma membrane Potassium Potassium - metabolism potassium channels Potassium Channels - genetics Potassium Channels - metabolism Potassium Channels - physiology Potassium Channels, Inwardly Rectifying - metabolism Potassium Channels, Inwardly Rectifying - physiology Potassium Chloride - metabolism Proteins stomatal movement |
| Title | Clustering of the K⁺ channel GORK of Arabidopsis parallels its gating by extracellular K |
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