The CaMKII holoenzyme structure in activation-competent conformations
Identifieur interne : 000B67 ( Main/Merge ); précédent : 000B66; suivant : 000B68The CaMKII holoenzyme structure in activation-competent conformations
Auteurs : Janette B. Myers [États-Unis] ; Vincent Zaegel [États-Unis] ; Steven J. Coultrap [États-Unis] ; Adam P. Miller [États-Unis] ; K. Ulrich Bayer [États-Unis] ; Steve L. Reichow [États-Unis]Source :
- Nature Communications [ 2041-1723 ] ; 2017.
Descripteurs français
- KwdFr :
- Activation enzymatique, Animaux, Calcium-Calmodulin-Dependent Protein Kinase Type 2 (), Calcium-Calmodulin-Dependent Protein Kinase Type 2 (génétique), Calcium-Calmodulin-Dependent Protein Kinase Type 2 (métabolisme), Conformation des protéines, Domaines protéiques, Humains, Microscopie électronique (), Modèles moléculaires, Multimérisation de protéines, Mutation, Phosphorylation, Rats, Transfert d'énergie par résonance de fluorescence.
- MESH :
- génétique : Calcium-Calmodulin-Dependent Protein Kinase Type 2.
- métabolisme : Calcium-Calmodulin-Dependent Protein Kinase Type 2.
- Activation enzymatique, Animaux, Calcium-Calmodulin-Dependent Protein Kinase Type 2, Conformation des protéines, Domaines protéiques, Humains, Microscopie électronique, Modèles moléculaires, Multimérisation de protéines, Mutation, Phosphorylation, Rats, Transfert d'énergie par résonance de fluorescence.
English descriptors
- KwdEn :
- Animals, Calcium-Calmodulin-Dependent Protein Kinase Type 2 (chemistry), Calcium-Calmodulin-Dependent Protein Kinase Type 2 (genetics), Calcium-Calmodulin-Dependent Protein Kinase Type 2 (metabolism), Enzyme Activation, Fluorescence Resonance Energy Transfer, Humans, Microscopy, Electron (methods), Models, Molecular, Mutation, Phosphorylation, Protein Conformation, Protein Domains, Protein Multimerization, Rats.
- MESH :
- chemical , chemistry : Calcium-Calmodulin-Dependent Protein Kinase Type 2.
- chemical , genetics : Calcium-Calmodulin-Dependent Protein Kinase Type 2.
- chemical , metabolism : Calcium-Calmodulin-Dependent Protein Kinase Type 2.
- methods : Microscopy, Electron.
- Animals, Enzyme Activation, Fluorescence Resonance Energy Transfer, Humans, Models, Molecular, Mutation, Phosphorylation, Protein Conformation, Protein Domains, Protein Multimerization, Rats.
Abstract
The Ca2+/calmodulin-dependent protein kinase II (CaMKII) assembles into large 12-meric holoenzymes, which is thought to enable regulatory processes required for synaptic plasticity underlying learning, memory and cognition. Here we used single particle electron microscopy (EM) to determine a pseudoatomic model of the CaMKIIα holoenzyme in an extended and activation-competent conformation. The holoenzyme is organized by a rigid central hub complex, while positioning of the kinase domains is highly flexible, revealing dynamic holoenzymes ranging from 15–35 nm in diameter. While most kinase domains are ordered independently, ∼20% appear to form dimers and <3% are consistent with a compact conformation. An additional level of plasticity is revealed by a small fraction of bona-fide 14-mers (<4%) that may enable subunit exchange. Biochemical and cellular FRET studies confirm that the extended state of CaMKIIα resolved by EM is the predominant form of the holoenzyme, even under molecular crowding conditions.
Url:
DOI: 10.1038/ncomms15742
PubMed: 28589927
PubMed Central: 5467236
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PMC:5467236Le document en format XML
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Reichow</name><affiliation wicri:level="1"><nlm:aff id="a1"><institution>Department of Chemistry, Portland State University</institution>, Portland, Oregon 97021,<country>USA</country></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author></analytic><series><title level="j">Nature Communications</title><idno type="eISSN">2041-1723</idno><imprint><date when="2017">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Calcium-Calmodulin-Dependent Protein Kinase Type 2 (chemistry)</term><term>Calcium-Calmodulin-Dependent Protein Kinase Type 2 (genetics)</term><term>Calcium-Calmodulin-Dependent Protein Kinase Type 2 (metabolism)</term><term>Enzyme Activation</term><term>Fluorescence Resonance Energy Transfer</term><term>Humans</term><term>Microscopy, Electron (methods)</term><term>Models, Molecular</term><term>Mutation</term><term>Phosphorylation</term><term>Protein Conformation</term><term>Protein Domains</term><term>Protein Multimerization</term><term>Rats</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Activation enzymatique</term><term>Animaux</term><term>Calcium-Calmodulin-Dependent Protein Kinase Type 2 ()</term><term>Calcium-Calmodulin-Dependent Protein Kinase Type 2 (génétique)</term><term>Calcium-Calmodulin-Dependent Protein Kinase Type 2 (métabolisme)</term><term>Conformation des protéines</term><term>Domaines protéiques</term><term>Humains</term><term>Microscopie électronique ()</term><term>Modèles moléculaires</term><term>Multimérisation de protéines</term><term>Mutation</term><term>Phosphorylation</term><term>Rats</term><term>Transfert d'énergie par résonance de fluorescence</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Calcium-Calmodulin-Dependent Protein Kinase Type 2</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Calcium-Calmodulin-Dependent Protein Kinase Type 2</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Calcium-Calmodulin-Dependent Protein Kinase Type 2</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Calcium-Calmodulin-Dependent Protein Kinase Type 2</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Microscopy, Electron</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Calcium-Calmodulin-Dependent Protein Kinase Type 2</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Enzyme Activation</term><term>Fluorescence Resonance Energy Transfer</term><term>Humans</term><term>Models, Molecular</term><term>Mutation</term><term>Phosphorylation</term><term>Protein Conformation</term><term>Protein Domains</term><term>Protein Multimerization</term><term>Rats</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Activation enzymatique</term><term>Animaux</term><term>Calcium-Calmodulin-Dependent Protein Kinase Type 2</term><term>Conformation des protéines</term><term>Domaines protéiques</term><term>Humains</term><term>Microscopie électronique</term><term>Modèles moléculaires</term><term>Multimérisation de protéines</term><term>Mutation</term><term>Phosphorylation</term><term>Rats</term><term>Transfert d'énergie par résonance de fluorescence</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>The Ca<sup>2+</sup>/calmodulin-dependent protein kinase II (CaMKII) assembles into large 12-meric holoenzymes, which is thought to enable regulatory processes required for synaptic plasticity underlying learning, memory and cognition. Here we used single particle electron microscopy (EM) to determine a pseudoatomic model of the CaMKIIα holoenzyme in an extended and activation-competent conformation. The holoenzyme is organized by a rigid central hub complex, while positioning of the kinase domains is highly flexible, revealing dynamic holoenzymes ranging from 15–35 nm in diameter. While most kinase domains are ordered independently, ∼20% appear to form dimers and <3% are consistent with a compact conformation. An additional level of plasticity is revealed by a small fraction of bona-fide 14-mers (<4%) that may enable subunit exchange. Biochemical and cellular FRET studies confirm that the extended state of CaMKIIα resolved by EM is the predominant form of the holoenzyme, even under molecular crowding conditions.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Coultrap, S J" uniqKey="Coultrap S">S. J. Coultrap</name></author><author><name sortKey="Bayer, K U" uniqKey="Bayer K">K. U. Bayer</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Lisman, J" uniqKey="Lisman J">J. Lisman</name></author><author><name sortKey="Yasuda, R" uniqKey="Yasuda R">R. Yasuda</name></author><author><name sortKey="Raghavachari, S" uniqKey="Raghavachari S">S. Raghavachari</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Hell, J W" uniqKey="Hell J">J. W. Hell</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Giese, K P" uniqKey="Giese K">K. P. Giese</name></author><author><name sortKey="Fedorov, N B" uniqKey="Fedorov N">N. B. Fedorov</name></author><author><name sortKey="Filipkowski, R K" uniqKey="Filipkowski R">R. K. Filipkowski</name></author><author><name sortKey="Silva, A J" uniqKey="Silva A">A. J. Silva</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Coultrap, S J" uniqKey="Coultrap S">S. J. Coultrap</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Bayer, K U" uniqKey="Bayer K">K. U. Bayer</name></author><author><name sortKey="De Koninck, P" uniqKey="De Koninck P">P. De Koninck</name></author><author><name sortKey="Leonard, A S" uniqKey="Leonard A">A. S. Leonard</name></author><author><name sortKey="Hell, J W" uniqKey="Hell J">J. W. Hell</name></author><author><name sortKey="Schulman, H" uniqKey="Schulman H">H. Schulman</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Barcomb, K" uniqKey="Barcomb K">K. Barcomb</name></author><author><name sortKey="Hell, J W" uniqKey="Hell J">J. W. Hell</name></author><author><name sortKey="Benke, T A" uniqKey="Benke T">T. A. Benke</name></author><author><name sortKey="Bayer, K U" uniqKey="Bayer K">K. U. 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Carter</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Smith, F D" uniqKey="Smith F">F. D. Smith</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Tang, G" uniqKey="Tang G">G. Tang</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Scheres, S H" uniqKey="Scheres S">S. H. Scheres</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Pettersen, E F" uniqKey="Pettersen E">E. F. Pettersen</name></author></analytic></biblStruct></listBibl></div1></back></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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