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Protein aggregation

  • RESEARCH ARTICLE
    Neurodegenerative disease-associated protein aggregates are poor inducers of the heat shock response in neuronal cells
    Rebecca San Gil, Dezerae Cox, Luke McAlary, Tracey Berg, Adam K. Walker, Justin J. Yerbury, Lezanne Ooi, Heath Ecroyd
    Journal of Cell Science 2020 133: jcs243709 doi: 10.1242/jcs.243709 Published 5 August 2020

    Summary: Aggregation-prone proteins associated with neurodegenerative diseases impair or evade the heat shock response in neuronal cells.

  • RESEARCH ARTICLE
    SOD1A4V aggregation alters ubiquitin homeostasis in a cell model of ALS
    Natalie E. Farrawell, Isabella Lambert-Smith, Kristen Mitchell, Jessie McKenna, Luke McAlary, Prajwal Ciryam, Kara L. Vine, Darren N. Saunders, Justin J. Yerbury
    Journal of Cell Science 2018 131: jcs209122 doi: 10.1242/jcs.209122 Published 12 June 2018

    Summary: Misfolded SOD1 contributes to ubiquitin proteasome system dysfunction in a cell model of ALS. Hence, ubiquitin homeostasis is an important marker of changes in ALS pathology.

  • RESEARCH ARTICLE
    PIGN prevents protein aggregation in the endoplasmic reticulum independently of its function in the GPI synthesis
    Shinji Ihara, Sohei Nakayama, Yoshiko Murakami, Emiko Suzuki, Masayo Asakawa, Taroh Kinoshita, Hitoshi Sawa
    Journal of Cell Science 2017 130: 602-613; doi: 10.1242/jcs.196717

    Summary: By using visualized secreted proteins markers, we identify that PIGN/PIGN-1 has an unexpected role in protein quality control preventing protein aggregation within the ER.

  • RESEARCH ARTICLE
    PrP-containing aggresomes are cytosolic components of an ER quality control mechanism
    Tatyana Dubnikov, Tziona Ben-Gedalya, Robert Reiner, Dominic Hoepfner, Wayne A. Cabral, Joan C. Marini, Ehud Cohen
    Journal of Cell Science 2016 129: 3635-3647; doi: 10.1242/jcs.186981

    Summary: Prion protein (PrP)-containing cytosolic aggresomes are components of a quality-control mechanism of the ER. PrP molecules that fail to enter the ER will not be deposited in pre-existing aggresomes.

  • RESEARCH ARTICLE
    Aggregation dynamics and identification of aggregation-prone mutants of the von Hippel–Lindau tumor suppressor protein
    Xavier Le Goff, Franck Chesnel, Olivier Delalande, Anne Couturier, Stéphane Dréano, Cathy Le Goff, Cécile Vigneau, Yannick Arlot-Bonnemains
    Journal of Cell Science 2016 129: 2638-2650; doi: 10.1242/jcs.184846

    Highlighted Article: If misfolded, the von Hippel–Lindau (pVHL) tumor suppressor protein is prone to aggregate and to be degraded. Tumorigenic mutations might compromise its folding. We identify new factors regulating pVHL folding.

  • RESEARCH ARTICLE
    Vulnerability of newly synthesized proteins to proteostasis stress
    Guilian Xu, Amrutha Pattamatta, Ryan Hildago, Michael C. Pace, Hilda Brown, David R. Borchelt
    Journal of Cell Science 2016 129: 1892-1901; doi: 10.1242/jcs.176479

    Summary: This study shows that stressors that burden the proteostatic network produce the greatest impact on newly made proteins with a substantial portion of the proteome being vulnerable to such stress.

  • 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 yeast peroxiredoxin Tsa1 protects against protein-aggregate-induced oxidative stress
    Alan J. Weids, Chris M. Grant
    Journal of Cell Science 2014 127: 1327-1335; doi: 10.1242/jcs.144022
  • RESEARCH ARTICLE
    Arsenite interferes with protein folding and triggers formation of protein aggregates in yeast
    Therese Jacobson, Clara Navarrete, Sandeep K. Sharma, Theodora C. Sideri, Sebastian Ibstedt, Smriti Priya, Chris M. Grant, Philipp Christen, Pierre Goloubinoff, Markus J. Tamás
    Journal of Cell Science 2012 125: 5073-5083; doi: 10.1242/jcs.107029

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