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Chaperone

  • RESEARCH ARTICLE
    An evolutionarily distinct chaperone promotes 20S proteasome α-ring assembly in plants
    Richard S. Marshall, David C. Gemperline, Fionn McLoughlin, Adam J. Book, Kay Hofmann, Richard D. Vierstra
    Journal of Cell Science 2020 133: jcs249862 doi: 10.1242/jcs.249862 Published 3 November 2020

    Highlighted Article: PBAC5 is an evolutionarily distinct chaperone that forms a tripartite complex with PBAC1 and PBAC2 to promote assembly of the 20S proteasome α-ring in Arabidopsis.

  • RESEARCH ARTICLE
    A trap mutant reveals the physiological client spectrum of TRC40
    Javier Coy-Vergara, Jhon Rivera-Monroy, Henning Urlaub, Christof Lenz, Blanche Schwappach
    Journal of Cell Science 2019 132: jcs230094 doi: 10.1242/jcs.230094 Published 1 July 2019

    Summary: A strategy to decipher which tail-anchored proteins do (as opposed to can or must) use the TRC pathway in intact cells generates a comprehensive list of human TRC40 clients.

  • RESEARCH ARTICLE
    Hsp70–Hsp110 chaperones deliver ubiquitin-dependent and -independent substrates to the 26S proteasome for proteolysis in yeast
    Ganapathi Kandasamy, Claes Andréasson
    Journal of Cell Science 2018 131: jcs210948 doi: 10.1242/jcs.210948 Published 20 March 2018

    Summary: Hsp110 associates with the proteasome and ensures the efficient delivery of Hsp70 chaperone-associated proteins for proteolysis in the yeast S. cerevisiae.

  • CELL SCIENCE AT A GLANCE
    BAG3-mediated proteostasis at a glance
    Christina Klimek, Barbara Kathage, Judith Wördehoff, Jörg Höhfeld
    Journal of Cell Science 2017 130: 2781-2788; doi: 10.1242/jcs.203679

    Summary: We discuss how the co-chaperone BAG3 maintains the proteome by balancing transcription, translation and autophagy, and how impairment or deregulation of BAG3 can cause muscle weakness, neurodegeneration and cancer.

  • TOOLS AND TECHNIQUES
    Distinguishing aggregate formation and aggregate clearance using cell-based assays
    Evelien Eenjes, Joanna M. Dragich, Harm H. Kampinga, Ai Yamamoto
    Journal of Cell Science 2016 129: 1260-1270; doi: 10.1242/jcs.179978

    Highlighted Article: Disequilibrium between aggregate formation and clearance leads to accumulation of aggregated proteins. We have created a new cell-based assay that can determine how modifiers can impact on aggregate burden.

  • RESEARCH ARTICLE
    The clathrin-binding and J-domains of GAK support the uncoating and chaperoning of clathrin by Hsc70 in the brain
    Bum-Chan Park, Yang-In Yim, Xiaohong Zhao, Maciej B. Olszewski, Evan Eisenberg, Lois E. Greene
    Journal of Cell Science 2015 128: 3811-3821; doi: 10.1242/jcs.171058

    Summary: Our studies on GAK- and auxilin-knockout mice show that the only essential domains of GAK and auxilin in the brain are the clathrin-binding domain and the J-domain that binds to Hsc70.

  • RESEARCH ARTICLE
    The structure of the complex between α‐tubulin, TBCE and TBCB reveals a tubulin dimer dissociation mechanism
    Marina Serna, Gerardo Carranza, Jaime Martín-Benito, Robert Janowski, Albert Canals, Miquel Coll, Juan Carlos Zabala, José María Valpuesta
    Journal of Cell Science 2015 128: 1824-1834; doi: 10.1242/jcs.167387
  • RESEARCH ARTICLE
    Assembly and quality control of the protein phosphatase 1 holoenzyme involves the Cdc48–Shp1 chaperone
    You-Liang Cheng, Rey-Huei Chen
    Journal of Cell Science 2015 128: 1180-1192; doi: 10.1242/jcs.165159
  • RESEARCH ARTICLE
    Scrib regulates HGF-mediated epithelial morphogenesis and is stabilized by Sgt1–HSP90
    Dennis J. Eastburn, Mirjam M. Zegers, Keith E. Mostov
    Journal of Cell Science 2012 125: 4147-4157; doi: 10.1242/jcs.108670
  • RESEARCH ARTICLE
    Functional domain mapping of peroxin Pex19p: interaction with Pex3p is essential for function and translocation
    Yuji Matsuzono, Takashi Matsuzaki, Yukio Fujiki
    Journal of Cell Science 2006 119: 3539-3550; doi: 10.1242/jcs.03100

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