Cancer Institute A national cancer institute
designated cancer center

Judith Frydman

Publication Details

  • Sorting out the trash: the spatial nature of eukaryotic protein quality control CURRENT OPINION IN CELL BIOLOGY Sontag, E. M., Vonk, W. I., Frydman, J. 2014; 26: 139-146

    Abstract:

    Failure to maintain protein homeostasis is associated with aggregation and cell death, and underies a growing list of pathologies including neurodegenerative diseases, aging, and cancer. Misfolded proteins can be toxic and interfere with normal cellular functions, particularly during proteotoxic stress. Accordingly, molecular chaperones, the ubiquitin-proteasome system (UPS) and autophagy together promote refolding or clearance of misfolded proteins. Here we discuss emerging evidence that the pathways of protein quality control (PQC) are intimately linked to cell architecture, and sequester proteins into spatially and functionally distinct PQC compartments. This sequestration serves a number of functions, including enhancing the efficiency of quality control; clearing the cellular milieu of potentially toxic species and facilitating asymmetric inheritance of damaged proteins to promote rejuvenation of daughter cells.

    View details for DOI 10.1016/j.ceb.2013.12.006

    View details for Web of Science ID 000331860400018

    View details for PubMedID 24463332

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