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Phosphatidylinositol 3-Phosphate Indirectly Activates KCa3.1 via 14 Amino Acids in the Carboxy Terminus of KCa3.1
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| Zeitschriftentitel: | Molecular Biology of the Cell |
|---|---|
| Personen und Körperschaften: | , , , , , , , |
| In: | Molecular Biology of the Cell, 17, 2006, 1, S. 146-154 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Society for Cell Biology (ASCB)
|
| Schlagwörter: |
| author_facet |
Srivastava, Shekhar Choudhury, Papiya Li, Zhai Liu, GongXin Nadkarni, Vivek Ko, Kyung Coetzee, William A. Skolnik, Edward Y. Srivastava, Shekhar Choudhury, Papiya Li, Zhai Liu, GongXin Nadkarni, Vivek Ko, Kyung Coetzee, William A. Skolnik, Edward Y. |
|---|---|
| author |
Srivastava, Shekhar Choudhury, Papiya Li, Zhai Liu, GongXin Nadkarni, Vivek Ko, Kyung Coetzee, William A. Skolnik, Edward Y. |
| spellingShingle |
Srivastava, Shekhar Choudhury, Papiya Li, Zhai Liu, GongXin Nadkarni, Vivek Ko, Kyung Coetzee, William A. Skolnik, Edward Y. Molecular Biology of the Cell Phosphatidylinositol 3-Phosphate Indirectly Activates KCa3.1 via 14 Amino Acids in the Carboxy Terminus of KCa3.1 Cell Biology Molecular Biology |
| author_sort |
srivastava, shekhar |
| spelling |
Srivastava, Shekhar Choudhury, Papiya Li, Zhai Liu, GongXin Nadkarni, Vivek Ko, Kyung Coetzee, William A. Skolnik, Edward Y. 1059-1524 1939-4586 American Society for Cell Biology (ASCB) Cell Biology Molecular Biology http://dx.doi.org/10.1091/mbc.e05-08-0763 <jats:p>KCa3.1 is an intermediate conductance Ca<jats:sup>2+</jats:sup>-activated K<jats:sup>+</jats:sup>channel that is expressed predominantly in hematopoietic cells, smooth muscle cells, and epithelia where it functions to regulate membrane potential, Ca<jats:sup>2+</jats:sup>influx, cell volume, and chloride secretion. We recently found that the KCa3.1 channel also specifically requires phosphatidylinositol-3 phosphate [PI(3)P] for channel activity and is inhibited by myotubularin-related protein 6 (MTMR6), a PI(3)P phosphatase. We now show that PI(3)P indirectly activates KCa3.1. Unlike KCa3.1 channels, the related KCa2.1, KCa2.2, or KCa2.3 channels do not require PI(3)P for activity, suggesting that the KCa3.1 channel has evolved a unique means of regulation that is critical for its biological function. By making chimeric channels between KCa3.1 and KCa2.3, we identified a stretch of 14 amino acids in the carboxy-terminal calmodulin binding domain of KCa3.1 that is sufficient to confer regulation of KCa2.3 by PI(3)P. However, mutation of a single potential phosphorylation site in these 14 amino acids did not affect channel activity. These data together suggest that PI(3)P and these 14 amino acids regulate KCa3.1 channel activity by recruiting an as yet to be defined regulatory subunit that is required for Ca<jats:sup>2+</jats:sup>gating of KCa3.1.</jats:p> Phosphatidylinositol 3-Phosphate Indirectly Activates KCa3.1 via 14 Amino Acids in the Carboxy Terminus of KCa3.1 Molecular Biology of the Cell |
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| title |
Phosphatidylinositol 3-Phosphate Indirectly Activates KCa3.1 via 14 Amino Acids in the Carboxy Terminus of KCa3.1 |
| title_unstemmed |
Phosphatidylinositol 3-Phosphate Indirectly Activates KCa3.1 via 14 Amino Acids in the Carboxy Terminus of KCa3.1 |
| title_full |
Phosphatidylinositol 3-Phosphate Indirectly Activates KCa3.1 via 14 Amino Acids in the Carboxy Terminus of KCa3.1 |
| title_fullStr |
Phosphatidylinositol 3-Phosphate Indirectly Activates KCa3.1 via 14 Amino Acids in the Carboxy Terminus of KCa3.1 |
| title_full_unstemmed |
Phosphatidylinositol 3-Phosphate Indirectly Activates KCa3.1 via 14 Amino Acids in the Carboxy Terminus of KCa3.1 |
| title_short |
Phosphatidylinositol 3-Phosphate Indirectly Activates KCa3.1 via 14 Amino Acids in the Carboxy Terminus of KCa3.1 |
| title_sort |
phosphatidylinositol 3-phosphate indirectly activates kca3.1 via 14 amino acids in the carboxy terminus of kca3.1 |
| topic |
Cell Biology Molecular Biology |
| url |
http://dx.doi.org/10.1091/mbc.e05-08-0763 |
| publishDate |
2006 |
| physical |
146-154 |
| description |
<jats:p>KCa3.1 is an intermediate conductance Ca<jats:sup>2+</jats:sup>-activated K<jats:sup>+</jats:sup>channel that is expressed predominantly in hematopoietic cells, smooth muscle cells, and epithelia where it functions to regulate membrane potential, Ca<jats:sup>2+</jats:sup>influx, cell volume, and chloride secretion. We recently found that the KCa3.1 channel also specifically requires phosphatidylinositol-3 phosphate [PI(3)P] for channel activity and is inhibited by myotubularin-related protein 6 (MTMR6), a PI(3)P phosphatase. We now show that PI(3)P indirectly activates KCa3.1. Unlike KCa3.1 channels, the related KCa2.1, KCa2.2, or KCa2.3 channels do not require PI(3)P for activity, suggesting that the KCa3.1 channel has evolved a unique means of regulation that is critical for its biological function. By making chimeric channels between KCa3.1 and KCa2.3, we identified a stretch of 14 amino acids in the carboxy-terminal calmodulin binding domain of KCa3.1 that is sufficient to confer regulation of KCa2.3 by PI(3)P. However, mutation of a single potential phosphorylation site in these 14 amino acids did not affect channel activity. These data together suggest that PI(3)P and these 14 amino acids regulate KCa3.1 channel activity by recruiting an as yet to be defined regulatory subunit that is required for Ca<jats:sup>2+</jats:sup>gating of KCa3.1.</jats:p> |
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| author | Srivastava, Shekhar, Choudhury, Papiya, Li, Zhai, Liu, GongXin, Nadkarni, Vivek, Ko, Kyung, Coetzee, William A., Skolnik, Edward Y. |
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| description | <jats:p>KCa3.1 is an intermediate conductance Ca<jats:sup>2+</jats:sup>-activated K<jats:sup>+</jats:sup>channel that is expressed predominantly in hematopoietic cells, smooth muscle cells, and epithelia where it functions to regulate membrane potential, Ca<jats:sup>2+</jats:sup>influx, cell volume, and chloride secretion. We recently found that the KCa3.1 channel also specifically requires phosphatidylinositol-3 phosphate [PI(3)P] for channel activity and is inhibited by myotubularin-related protein 6 (MTMR6), a PI(3)P phosphatase. We now show that PI(3)P indirectly activates KCa3.1. Unlike KCa3.1 channels, the related KCa2.1, KCa2.2, or KCa2.3 channels do not require PI(3)P for activity, suggesting that the KCa3.1 channel has evolved a unique means of regulation that is critical for its biological function. By making chimeric channels between KCa3.1 and KCa2.3, we identified a stretch of 14 amino acids in the carboxy-terminal calmodulin binding domain of KCa3.1 that is sufficient to confer regulation of KCa2.3 by PI(3)P. However, mutation of a single potential phosphorylation site in these 14 amino acids did not affect channel activity. These data together suggest that PI(3)P and these 14 amino acids regulate KCa3.1 channel activity by recruiting an as yet to be defined regulatory subunit that is required for Ca<jats:sup>2+</jats:sup>gating of KCa3.1.</jats:p> |
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| spelling | Srivastava, Shekhar Choudhury, Papiya Li, Zhai Liu, GongXin Nadkarni, Vivek Ko, Kyung Coetzee, William A. Skolnik, Edward Y. 1059-1524 1939-4586 American Society for Cell Biology (ASCB) Cell Biology Molecular Biology http://dx.doi.org/10.1091/mbc.e05-08-0763 <jats:p>KCa3.1 is an intermediate conductance Ca<jats:sup>2+</jats:sup>-activated K<jats:sup>+</jats:sup>channel that is expressed predominantly in hematopoietic cells, smooth muscle cells, and epithelia where it functions to regulate membrane potential, Ca<jats:sup>2+</jats:sup>influx, cell volume, and chloride secretion. We recently found that the KCa3.1 channel also specifically requires phosphatidylinositol-3 phosphate [PI(3)P] for channel activity and is inhibited by myotubularin-related protein 6 (MTMR6), a PI(3)P phosphatase. We now show that PI(3)P indirectly activates KCa3.1. Unlike KCa3.1 channels, the related KCa2.1, KCa2.2, or KCa2.3 channels do not require PI(3)P for activity, suggesting that the KCa3.1 channel has evolved a unique means of regulation that is critical for its biological function. By making chimeric channels between KCa3.1 and KCa2.3, we identified a stretch of 14 amino acids in the carboxy-terminal calmodulin binding domain of KCa3.1 that is sufficient to confer regulation of KCa2.3 by PI(3)P. However, mutation of a single potential phosphorylation site in these 14 amino acids did not affect channel activity. These data together suggest that PI(3)P and these 14 amino acids regulate KCa3.1 channel activity by recruiting an as yet to be defined regulatory subunit that is required for Ca<jats:sup>2+</jats:sup>gating of KCa3.1.</jats:p> Phosphatidylinositol 3-Phosphate Indirectly Activates KCa3.1 via 14 Amino Acids in the Carboxy Terminus of KCa3.1 Molecular Biology of the Cell |
| spellingShingle | Srivastava, Shekhar, Choudhury, Papiya, Li, Zhai, Liu, GongXin, Nadkarni, Vivek, Ko, Kyung, Coetzee, William A., Skolnik, Edward Y., Molecular Biology of the Cell, Phosphatidylinositol 3-Phosphate Indirectly Activates KCa3.1 via 14 Amino Acids in the Carboxy Terminus of KCa3.1, Cell Biology, Molecular Biology |
| title | Phosphatidylinositol 3-Phosphate Indirectly Activates KCa3.1 via 14 Amino Acids in the Carboxy Terminus of KCa3.1 |
| title_full | Phosphatidylinositol 3-Phosphate Indirectly Activates KCa3.1 via 14 Amino Acids in the Carboxy Terminus of KCa3.1 |
| title_fullStr | Phosphatidylinositol 3-Phosphate Indirectly Activates KCa3.1 via 14 Amino Acids in the Carboxy Terminus of KCa3.1 |
| title_full_unstemmed | Phosphatidylinositol 3-Phosphate Indirectly Activates KCa3.1 via 14 Amino Acids in the Carboxy Terminus of KCa3.1 |
| title_short | Phosphatidylinositol 3-Phosphate Indirectly Activates KCa3.1 via 14 Amino Acids in the Carboxy Terminus of KCa3.1 |
| title_sort | phosphatidylinositol 3-phosphate indirectly activates kca3.1 via 14 amino acids in the carboxy terminus of kca3.1 |
| title_unstemmed | Phosphatidylinositol 3-Phosphate Indirectly Activates KCa3.1 via 14 Amino Acids in the Carboxy Terminus of KCa3.1 |
| topic | Cell Biology, Molecular Biology |
| url | http://dx.doi.org/10.1091/mbc.e05-08-0763 |