Structure of native lens connexin 46/50 intercellular channels by cryo-EM

Janette B. Myers, Bassam G. Haddad, Susan E. O’Neill, Dror S. Chorev, Craig C. Yoshioka, Carol V. Robinson, Daniel M. Zuckerman and Steve L. Reichow ()
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Janette B. Myers: Portland State University
Bassam G. Haddad: Portland State University
Susan E. O’Neill: Portland State University
Dror S. Chorev: University of Oxford
Craig C. Yoshioka: Oregon Health and Science University
Carol V. Robinson: University of Oxford
Daniel M. Zuckerman: Oregon Health and Science University
Steve L. Reichow: Portland State University

Nature, 2018, vol. 564, issue 7736, 372-377

Abstract: Abstract Gap junctions establish direct pathways for cell-to-cell communication through the assembly of twelve connexin subunits that form intercellular channels connecting neighbouring cells. Co-assembly of different connexin isoforms produces channels with unique properties and enables communication across cell types. Here we used single-particle cryo-electron microscopy to investigate the structural basis of connexin co-assembly in native lens gap junction channels composed of connexin 46 and connexin 50 (Cx46/50). We provide the first comparative analysis to connexin 26 (Cx26), which—together with computational studies—elucidates key energetic features governing gap junction permselectivity. Cx46/50 adopts an open-state conformation that is distinct from the Cx26 crystal structure, yet it appears to be stabilized by a conserved set of hydrophobic anchoring residues. ‘Hot spots’ of genetic mutations linked to hereditary cataract formation map to the core structural–functional elements identified in Cx46/50, suggesting explanations for many of the disease-causing effects.

Date: 2018
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DOI: 10.1038/s41586-018-0786-7

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