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TitleStructures of wild-type and selected CMT1X mutant connexin 32 gap junction channels and hemichannels.
Journal, issue, pagesSci Adv, Vol. 9, Issue 35, Page eadh4890, Year 2023
Publish dateAug 30, 2023
AuthorsChao Qi / Pia Lavriha / Erva Bayraktar / Anand Vaithia / Dina Schuster / Micaela Pannella / Valentina Sala / Paola Picotti / Mario Bortolozzi / Volodymyr M Korkhov /
PubMed AbstractIn myelinating Schwann cells, connection between myelin layers is mediated by gap junction channels (GJCs) formed by docked connexin 32 (Cx32) hemichannels (HCs). Mutations in Cx32 cause the X-linked ...In myelinating Schwann cells, connection between myelin layers is mediated by gap junction channels (GJCs) formed by docked connexin 32 (Cx32) hemichannels (HCs). Mutations in Cx32 cause the X-linked Charcot-Marie-Tooth disease (CMT1X), a degenerative neuropathy without a cure. A molecular link between Cx32 dysfunction and CMT1X pathogenesis is still missing. Here, we describe the high-resolution cryo-electron cryo-myography (cryo-EM) structures of the Cx32 GJC and HC, along with two CMT1X-linked mutants, W3S and R22G. While the structures of wild-type and mutant GJCs are virtually identical, the HCs show a major difference: In the W3S and R22G mutant HCs, the amino-terminal gating helix partially occludes the pore, consistent with a diminished HC activity. Our results suggest that HC dysfunction may be involved in the pathogenesis of CMT1X.
External linksSci Adv / PubMed:37647412 / PubMed Central
MethodsEM (single particle)
Resolution2.14 - 3.53 Å
Structure data

15010

7zxm

EMDB-15010, PDB-7zxm:
cryo-EM structure of Connexin 32 gap junction channel
Method: EM (single particle) / Resolution: 2.14 Å

15011

7zxn

EMDB-15011, PDB-7zxn:
cryo-EM structure of Connexin 32 gap junction channel
Method: EM (single particle) / Resolution: 3.06 Å

15012

7zxo

EMDB-15012, PDB-7zxo:
cryo-EM structure of Connexin 32 gap junction channel
Method: EM (single particle) / Resolution: 2.5 Å

15013

7zxp

EMDB-15013, PDB-7zxp:
cryo-EM structure of Connexin 32 R22G mutation gap junction channel
Method: EM (single particle) / Resolution: 2.39 Å

15014

7zxq

EMDB-15014, PDB-7zxq:
cryo-EM structure of Connexin 32 R22G mutation hemi channel
Method: EM (single particle) / Resolution: 3.53 Å

15016

7zxt

EMDB-15016, PDB-7zxt:
cryo-EM structure of Connexin 32 W3S mutation hemi channel
Method: EM (single particle) / Resolution: 2.9 Å

Chemicals

ChemComp-CLR:
CHOLESTEROL

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / connexin / gap junction channel / cell communication / Hemi channel

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