Full metadata record
DC Field | Value | Language |
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dc.contributor.author | Suh, BC[Suh, Byung-Chang] | ko |
dc.contributor.author | Kim, DI[Kim, Dong-Il] | ko |
dc.contributor.author | Falkenburger, BH[Falkenburger, Bjoern H.] | ko |
dc.contributor.author | Hille, B[Hille, Bertil] | ko |
dc.date.available | 2017-05-11T02:10:28Z | - |
dc.date.created | 2017-04-10 | - |
dc.date.issued | 2012-02-21 | - |
dc.identifier.citation | Proceedings of the National Academy of Sciences of the United States of America, v.109, no.8, pp.3161 - 3166 | - |
dc.identifier.issn | 0027-8424 | - |
dc.identifier.uri | http://hdl.handle.net/20.500.11750/1714 | - |
dc.description.abstract | The β-subunits of voltage-gated Ca 2+ (Ca V) channels regulate the functional expression and several biophysical properties of high-voltage-activated Ca V channels. We find that Ca V β-subunits also determine channel regulation by the membrane phospholipid phosphatidylinositol 4,5-bisphosphate (PIP 2). When Ca V1.3, -2.1, or -2.2 channels are cotransfected with the β3-subunit, a cytosolic protein, they can be inhibited by activating a voltage-sensitive lipid phosphatase to deplete PIP 2. When these channels are coexpressed with a β2a-subunit, a palmitoylated peripheral membrane protein, the inhibition is much smaller. PIP 2 sensitivity could be increased by disabling the two palmitoylation sites in the β2a-subunit. To further test effects of membrane targeting of Ca V β-subunits on PIP 2 regulation, the N terminus of Lyn was ligated onto the cytosolic β3-subunit to confer lipidation. This chimera, like the Ca V β2a-subunit, displayed plasma membrane localization, slowed the inactivation of Ca V2.2 channels, and increased the current density. In addition, the Lyn-β3 subunit significantly decreased Ca Vchannel inhibition by PIP 2 depletion. Evidently lipidation and membrane anchoring of Ca V β-subunits compete with the PIP 2 regulation of high-voltage-activated Ca V channels. Compared with expression with Ca V β3-subunits alone, inhibition of Ca V2.2 channels by PIP 2 depletion could be significantly attenuated when β2a was coexpressed with β3. Our data suggest that the Ca V currents in neurons would be regulated by membrane PIP 2 to a degree that depends on their endogenous β-subunit combinations. | - |
dc.publisher | National Academy of Sciences | - |
dc.subject | Amino Terminal Sequence | - |
dc.subject | Animals | - |
dc.subject | Calcium Channels | - |
dc.subject | Calcium Current | - |
dc.subject | Cell Membrane | - |
dc.subject | Chimeric Protein | - |
dc.subject | Controlled Study | - |
dc.subject | Enzyme Activation | - |
dc.subject | Genetic Transfection | - |
dc.subject | HEK293 Cells | - |
dc.subject | Humans | - |
dc.subject | Ion Channel Gating | - |
dc.subject | Lipoylation | - |
dc.subject | M1 Muscarinic Receptor | - |
dc.subject | Nerve Cell | - |
dc.subject | Palmitoylation | - |
dc.subject | Phosphatidylinositol 4,5-Diphosphate | - |
dc.subject | Phosphatidylinositol 4,5 Bisphosphate | - |
dc.subject | Phosphoprotein Phosphatases | - |
dc.subject | Priority Journal | - |
dc.subject | Protein Kinase Lyn | - |
dc.subject | Protein Subunit | - |
dc.subject | Protein Subunits | - |
dc.subject | Protein Transport | - |
dc.subject | Regulatory Mechanism | - |
dc.subject | Unclassified Drug | - |
dc.subject | Voltage-Gated Calcium Channel | - |
dc.subject | Voltage-Gated Calcium Channel 1.3 | - |
dc.subject | Voltage-Gated Calcium Channel 2.1 | - |
dc.subject | Voltage-Gated Calcium Channel 2.2 | - |
dc.subject | Voltage-Gated Calcium Channel Beta2A Subunit | - |
dc.subject | Voltage-Gated Calcium Channel Beta3 Subunit | - |
dc.subject | Voltage-Sensing Phosphatase | - |
dc.subject | Zebrafish | - |
dc.title | Membrane-localized beta-subunits alter the PIP2 regulation of high-voltage activated Ca2+ channels | - |
dc.type | Article | - |
dc.identifier.doi | 10.1073/pnas.1121434109 | - |
dc.identifier.wosid | 000300495100094 | - |
dc.identifier.scopusid | 2-s2.0-84863148751 | - |
dc.type.local | Article(Overseas) | - |
dc.type.rims | ART | - |
dc.description.journalClass | 1 | - |
dc.contributor.nonIdAuthor | Falkenburger, BH[Falkenburger, Bjoern H.] | - |
dc.contributor.nonIdAuthor | Hille, B[Hille, Bertil] | - |
dc.identifier.citationVolume | 109 | - |
dc.identifier.citationNumber | 8 | - |
dc.identifier.citationStartPage | 3161 | - |
dc.identifier.citationEndPage | 3166 | - |
dc.identifier.citationTitle | Proceedings of the National Academy of Sciences of the United States of America | - |
dc.type.journalArticle | Article | - |
dc.contributor.affiliatedAuthor | Suh, BC[Suh, Byung-Chang] | - |
dc.contributor.affiliatedAuthor | Kim, DI[Kim, Dong-Il] | - |
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