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Protein targeting and degradation are coupled for elimination of mislocalized proteins

Author

Listed:
  • Tara Hessa

    (Cell Biology and Metabolism Program, National Institute of Child Health and Human Development, National Institutes of Health)

  • Ajay Sharma

    (Cell Biology and Metabolism Program, National Institute of Child Health and Human Development, National Institutes of Health)

  • Malaiyalam Mariappan

    (Cell Biology and Metabolism Program, National Institute of Child Health and Human Development, National Institutes of Health)

  • Heather D. Eshleman

    (Cell Biology and Metabolism Program, National Institute of Child Health and Human Development, National Institutes of Health
    Present addresses: Department of Physiology, University of California, San Francisco, California 94158, USA (H.D.E.); MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK (R.S.H.).)

  • Erik Gutierrez

    (Cell Biology and Metabolism Program, National Institute of Child Health and Human Development, National Institutes of Health
    Johns Hopkins University)

  • Ramanujan S. Hegde

    (Cell Biology and Metabolism Program, National Institute of Child Health and Human Development, National Institutes of Health
    Present addresses: Department of Physiology, University of California, San Francisco, California 94158, USA (H.D.E.); MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK (R.S.H.).)

Abstract

Removal of 'spare' proteins Membrane proteins that fail to be delivered to the endoplasmic reticulum must be rapidly degraded to avoid inappropriate aggregation and disruption of protein homeostasis. The mechanism of this process of mislocalized protein (MLP) degradation is unknown. Here Bag6, a chaperone complex involved in protein targeting, is identified as part of this mechanism. Bag6 interacts with and captures MLPs, coupling them to the ubiquitin-mediated degradation pathway. This could potentially achieve rapid degradation of MLPs without futile engagement of the cytosolic folding machinery.

Suggested Citation

  • Tara Hessa & Ajay Sharma & Malaiyalam Mariappan & Heather D. Eshleman & Erik Gutierrez & Ramanujan S. Hegde, 2011. "Protein targeting and degradation are coupled for elimination of mislocalized proteins," Nature, Nature, vol. 475(7356), pages 394-397, July.
    • Handle: RePEc:nat:nature:v:475:y:2011:i:7356:d:10.1038_nature10181
    DOI: 10.1038/nature10181
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    Cited by:

    1. Morgane Boone & Pathmanaban Ramasamy & Jasper Zuallaert & Robbin Bouwmeester & Berre Moer & Davy Maddelein & Demet Turan & Niels Hulstaert & Hannah Eeckhaut & Elien Vandermarliere & Lennart Martens & , 2021. "Massively parallel interrogation of protein fragment secretability using SECRiFY reveals features influencing secretory system transit," Nature Communications, Nature, vol. 12(1), pages 1-16, December.
    2. Bayan Mashahreh & Shir Armony & Kristoffer Enøe Johansson & Alon Chappleboim & Nir Friedman & Richard G. Gardner & Rasmus Hartmann-Petersen & Kresten Lindorff-Larsen & Tommer Ravid, 2022. "Conserved degronome features governing quality control associated proteolysis," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    3. Sylvia Hartmann & Claudia Döring & Christina Jakobus & Benjamin Rengstl & Sebastian Newrzela & Thomas Tousseyn & Xavier Sagaert & Maurilio Ponzoni & Fabio Facchetti & Chris de Wolf-Peeters & Christian, 2013. "Nodular Lymphocyte Predominant Hodgkin Lymphoma and T Cell/Histiocyte Rich Large B Cell Lymphoma - Endpoints of a Spectrum of One Disease?," PLOS ONE, Public Library of Science, vol. 8(11), pages 1-10, November.

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