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Protein Quality Control at Membranes

New Content ItemGuest Editors: Anne Bertolotti, Ramanujan Hegde, Peter Walter, Jonathan Weissman

Cells employ stringent quality control processes to ensure appropriate folding of proteins, which – if misfolded – could disrupt cell functions and lead to disease. Many of these strategies take place at cellular membranes, whose hydrophobic environment provides an additional challenge.

For this series BMC Biology have invited Reviews and Q&As on how protein quality control is ensured at membranes, as well as why protein quality control is needed in the first place.

The series is open for submission of research articles that bring fresh insights into the causes and consequences of protein misfolding at membranes, as well as papers that report new methods or techniques of broad interest. 

Papers in our Registered Reports format will also be welcomed.

Submit your manuscript here

Please use the online submission system, and indicate in your covering letter that you would like the manuscript to be considered for the “Protein Quality Control at Membranes” series. If you would like to inquire about the suitability of a manuscript for consideration, please email a pre-submission inquiry to 


Protein Misfolding – Protein Quality Control – Chaperones – Ubiquitination – Protein Translocation – Protein Energy Landscapes – Proteotoxicity – Unfolded Protein Response – ER Associated Degradation – Membrane targeting – Autophagy – Co-Translational Folding

“Image created by Bob Schiffrin (Astbury Centre for Structural Molecular Biology, University of Leeds); adapted from Bob Schiffrin, David Brockwell, and Sheena Radford’s review in this series: Outer membrane protein folding from an energy landscape perspective, BMC Biology, 2017” 

  1. The mitochondrial intermembrane space (IMS) is home to proteins fulfilling numerous essential cellular processes, particularly in metabolism and mitochondrial function. All IMS proteins are nuclear encoded and...

    Authors: Lena Maria Murschall, Anne Gerhards, Thomas MacVicar, Esra Peker, Lidwina Hasberg, Stephan Wawra, Thomas Langer and Jan Riemer
    Citation: BMC Biology 2020 18:96
  2. Protein quality control mechanisms are essential for cell health and involve delivery of proteins to specific cellular compartments for recycling or degradation. In particular, stray hydrophobic proteins are c...

    Authors: Santiago Martínez-Lumbreras, Ewelina M. Krysztofinska, Arjun Thapaliya, Alessandro Spilotros, Dijana Matak-Vinkovic, Enrico Salvadori, Peristera Roboti, Yvonne Nyathi, Janina H. Muench, Maxie M. Roessler, Dmitri I. Svergun, Stephen High and Rivka L. Isaacson
    Citation: BMC Biology 2018 16:76
  3. The proteome of mitochondria comprises mostly proteins that originate as precursors in the cytosol. Before import into the organelle, such proteins are exposed to cytosolic quality control mechanisms. Multiple...

    Authors: Lukasz Kowalski, Piotr Bragoszewski, Anton Khmelinskii, Edyta Glow, Michael Knop and Agnieszka Chacinska
    Citation: BMC Biology 2018 16:66

    The Commentary to this article has been published in BMC Biology 2018 16:63

  4. Tandem fluorescent protein timers are elegant tools to determine proteolytic stabilities of cytosolic proteins with high spatial and temporal resolution. In a new study published in BMC Biology, Kowalski et al. f...

    Authors: Eva Zöller, R. Todd Alexander and Johannes M. Herrmann
    Citation: BMC Biology 2018 16:63

    The original article was published in BMC Biology 2018 16:66

  5. Developmental pathways must be responsive to the environment. Phosphorylation of eIF2α enables a family of stress-sensing kinases to trigger the integrated stress response (ISR), which has pro-survival and dev...

    Authors: Elke Malzer, Caia S. Dominicus, Joseph E. Chambers, Jennifer A. Dickens, Souradip Mookerjee and Stefan J. Marciniak
    Citation: BMC Biology 2018 16:34
  6. Caenorhabditis elegans neurons have recently been found to throw out cellular debris for remote degradation and/or storage, adding an “extracellular garbage elimination” option to known intracellular protein and ...

    Authors: Meghan Lee Arnold, Ilija Melentijevic, Anna Joelle Smart and Monica Driscoll
    Citation: BMC Biology 2018 16:17
  7. Efficient movement of proteins across membranes is required for cell health. The translocation process is particularly challenging when the channel in the membrane through which proteins must pass is narrow—su...

    Authors: Elizabeth A. Craig
    Citation: BMC Biology 2018 16:11
  8. The efficient production, folding, and secretion of proteins is critical for cancer cell survival. However, cancer cells thrive under stress conditions that damage proteins, so many cancer cells overexpress mo...

    Authors: Sara Sannino and Jeffrey L. Brodsky
    Citation: BMC Biology 2017 15:109
  9. Many proteins of the mitochondrial intermembrane space (IMS) contain structural disulfide bonds formed by the mitochondrial disulfide relay. In fungi and animals, the sulfhydryl oxidase Erv1 ‘generates’ disulf...

    Authors: Valentina Peleh, Flavien Zannini, Sandra Backes, Nicolas Rouhier and Johannes M. Herrmann
    Citation: BMC Biology 2017 15:106