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TitleEMC chaperone-Ca structure reveals an ion channel assembly intermediate.
Journal, issue, pagesNature, Vol. 619, Issue 7969, Page 410-419, Year 2023
Publish dateMay 17, 2023
AuthorsZhou Chen / Abhisek Mondal / Fayal Abderemane-Ali / Seil Jang / Sangeeta Niranjan / José L Montaño / Balyn W Zaro / Daniel L Minor /
PubMed AbstractVoltage-gated ion channels (VGICs) comprise multiple structural units, the assembly of which is required for function. Structural understanding of how VGIC subunits assemble and whether chaperone ...Voltage-gated ion channels (VGICs) comprise multiple structural units, the assembly of which is required for function. Structural understanding of how VGIC subunits assemble and whether chaperone proteins are required is lacking. High-voltage-activated calcium channels (Cas) are paradigmatic multisubunit VGICs whose function and trafficking are powerfully shaped by interactions between pore-forming Ca1 or Ca2 Caα (ref. ), and the auxiliary Caβ and Caαδ subunits. Here we present cryo-electron microscopy structures of human brain and cardiac Ca1.2 bound with Caβ to a chaperone-the endoplasmic reticulum membrane protein complex (EMC)-and of the assembled Ca1.2-Caβ-Caαδ-1 channel. These structures provide a view of an EMC-client complex and define EMC sites-the transmembrane (TM) and cytoplasmic (Cyto) docks; interaction between these sites and the client channel causes partial extraction of a pore subunit and splays open the Caαδ-interaction site. The structures identify the Caαδ-binding site for gabapentinoid anti-pain and anti-anxiety drugs, show that EMC and Caαδ interactions with the channel are mutually exclusive, and indicate that EMC-to-Caαδ hand-off involves a divalent ion-dependent step and Ca1.2 element ordering. Disruption of the EMC-Ca complex compromises Ca function, suggesting that the EMC functions as a channel holdase that facilitates channel assembly. Together, the structures reveal a Ca assembly intermediate and EMC client-binding sites that could have wide-ranging implications for the biogenesis of VGICs and other membrane proteins.
External linksNature / PubMed:37196677 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 3.6 Å
Structure data

28375

8eog

EMDB-28375: Structure of the human L-type voltage-gated calcium channel Cav1.2 complexed with L-leucine (CABAD Map 2)
PDB-8eog: Structure of the human L-type voltage-gated calcium channel Cav1.2 complexed with L-leucine
Method: EM (single particle) / Resolution: 3.3 Å

28376

8eoi

EMDB-28376: Structure of a human EMC:human Cav1.2 channel complex in GDN detergent (ECAB Map 3)
PDB-8eoi: Structure of a human EMC:human Cav1.2 channel complex in GDN detergent
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-28561: Human L-type voltage-gated calcium channel Cav1.2 complexed with L-leucine (Segment Map 01)
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-28564: Human L-type voltage-gated calcium channel Cav1.2 complexed with L-leucine (Segment Map 02)
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-28578: Human EMC:human Cav1.2 channel complex (Segment map 01)
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-28579: Human EMC:human Cav1.2 channel complex in GDN detergent (Segment map 02)
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-40559: Human EMC:human Cav1.2 channel complex in GDN detergent (ECAB Map 1, Consensus Map)
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-40560: Human EMC:human Cav1.2 channel complex in GDN detergent (ECAB Map 2, Consensus Map)
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-40561: Human L-type voltage-gated calcium channel Cav1.2 (CABAD Map 1, Consensus Map)
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-CA:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-LEU:
LEUCINE / Leucine

ChemComp-CLR:
CHOLESTEROL / Cholesterol

ChemComp-WNZ:
(2R)-3-{[(R)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(dodecanoyloxy)propyl dodecanoate

ChemComp-WO9:
(2R)-3-{[(R)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(dodecanoyloxy)propyl heptadecanoate

ChemComp-HOH:
WATER / Water

ChemComp-9Z9:
(3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en / detergent*YM

Source
  • homo sapiens (human)
  • oryctolagus cuniculus (rabbit)
KeywordsMEMBRANE PROTEIN / voltage-gated calcium channel / CaV alpha2delta / drug binding / gabapentinoid / endoplasmic reticulum membrane protein complex / holdase / biogenesis

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