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Showing 1–12 of 12 results
Advanced filters: Author: Steve L. Reichow Clear advanced filters

  • Gap junctions close in response to intracellular acidification. Using cryo-EM, the authors reveal a reversible gating mechanism in Cx46/50, where lipid entry into the pore displaces a gating helix and induces pH-dependent conformational closure.

    • Joshua M. Jarodsky
    • Janette B. Myers
    • Steve L. Reichow
    ResearchOpen Access
    Nature Communications
    P: 1-16

  • High-resolution cryo-EM structures of a small heat shock protein reveal how client-induced scaffold destabilization promotes polydispersed higher-order assembly and cooperative sequestration, revealing insight into the structural basis of sHSP chaperone function under cell stress.

    • Adam P. Miller
    • Steve L. Reichow
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-12

  • The local lipid environment is known to affect the structure, stability and intercellular channel activity of gap junctions, however, the molecular basis for these effects remains unknown. Here authors report the CryoEM structure of Cx46/50 lipid-embedded channels, by which they reveal a lipid-induced stabilization to the channel.

    • Jonathan A. Flores
    • Bassam G. Haddad
    • Steve L. Reichow
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-11

  • Here the authors show that mutating αB-crystallin’s NT-IXI motif transforms polydispersed oligomers into ordered fibrils, enabling cryo-EM to provide insights into the principles of high-order assembly and molecular plasticity of small heat shock proteins.

    • Russell McFarland
    • Rozhan Noroozi
    • Steve L. Reichow
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-15

  • Calmodulin (CaM) regulates a variety of membrane channels in response to Ca2+, but the precise mechanisms are still unclear. Now a combination of single-particle EM, molecular dynamics simulations and functional assays is used to elucidate the structure of Ca2+–CaM bound to the full-length aquaporin AQP0, revealing a cytoplasmic gate that is closed upon CaM binding to control channel permeability in an allosteric manner.

    • Steve L Reichow
    • Daniel M Clemens
    • Tamir Gonen
    Research
    Nature Structural & Molecular Biology
    Volume: 20, P: 1085-1092

  • Secretins are bacterial outer membrane proteins involved in different pathways for protein secretion or macromolecular complex assembly. Secretin can form a large oligomeric pore, whose opening needs to be carefully regulated. Now cryo-EM analysis of the Vibrio cholerae secretin GspD reveals a closed channel, with a constricted periplasmic vestibule, offering insight into the mechanism of GspD opening during protein secretion.

    • Steve L Reichow
    • Konstantin V Korotkov
    • Tamir Gonen
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 1226-1232

  • Cryo-electron microscopy structures of connexin channels composed of connexin 46 and connexin 50 in an open-state reveal features that govern permselectivity and the location of mutated residues linked to herediatry cataracts.

    • Janette B. Myers
    • Bassam G. Haddad
    • Steve L. Reichow
    Research
    Nature
    Volume: 564, P: 372-377

  • Ca2+/calmodulin-dependent protein kinase II (CaMKII) forms a 12 subunit holoenzyme central to synaptic plasticity. Here the authors report a 3D structure of the CaMKII holoenzyme in an activation-competent state obtained by single particle EM, and suggest a role for the intrinsically disordered linker domain in facilitating cooperative activation.

    • Janette B. Myers
    • Vincent Zaegel
    • Steve L. Reichow
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-15

  • The co-transcriptional processing of RNA depends on the precisely timed recruitment of different factors to the elongating transcript, which depends on the phosphorylation state of the C-terminal domain (CTD) of RNA polymerase II. Varani and coworkers show that two transcription termination factors, Rtt103 and Pcf1, bind specifically and cooperatively to Ser2-phosphorylated CTD. This provides a way to ensure that proper polyadenylation occurs only where Ser2 phosphorylation density is highest.

    • Bradley M Lunde
    • Steve L Reichow
    • Gabriele Varani
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 1195-1201

  • The kinetochore is a large protein complex that assembles on centromeric DNA and captures microtubules to mediate chromosome separation. These authors report the first purification of functional kinetochores. They also show that kinetochore particles maintain load-bearing associations with assembling and disassembling ends of single microtubules and that tension increases the lifetimes of the attachments directly. These results provide evidence that tension selectively stabilises kinetochore–microtubule interactions.

    • Bungo Akiyoshi
    • Krishna K. Sarangapani
    • Sue Biggins
    Research
    Nature
    Volume: 468, P: 576-579