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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

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Volume 396, Issue 9-10


Homeostatic control of biological membranes by dedicated lipid and membrane packing sensors

Kristina Puth
  • Institute of Biochemistry, Buchmann Institute for Molecular Life Sciences, Goethe University Frankfurt, Max-von-Laue-Str. 15, D-60438 Frankfurt/Main, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Harald F. Hofbauer
  • Institute of Biochemistry, Buchmann Institute for Molecular Life Sciences, Goethe University Frankfurt, Max-von-Laue-Str. 15, D-60438 Frankfurt/Main, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ James P. Sáenz / Robert Ernst
  • Corresponding author
  • Institute of Biochemistry, Buchmann Institute for Molecular Life Sciences, Goethe University Frankfurt, Max-von-Laue-Str. 15, D-60438 Frankfurt/Main, Germany
  • Email
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2015-04-03 | DOI: https://doi.org/10.1515/hsz-2015-0130


Biological membranes are dynamic and complex assemblies of lipids and proteins. Eukaryotic lipidomes encompass hundreds of distinct lipid species and we have only begun to understand their role and function. This review focuses on recent advances in the field of lipid sensors and discusses methodical approaches to identify and characterize putative sensor domains. We elaborate on the role of integral and conditionally membrane-associated sensor proteins, their molecular mechanisms, and identify open questions in the emerging field of membrane homeostasis.

Keywords: lipid bilayer stress; lipid sensing; membrane homeostasis; membrane stress response; OLE pathway; unfolded protein response (UPR)


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About the article

Kristina Puth

Kristina Puth studied Biochemistry at the Goethe University Frankfurt and received her Diploma in 2012. Since 2012, she has been a PhD student in the Molecular Membrane Biology group at the Goethe University Frankfurt and had focused her PhD on the molecular basis of lipid-induced ER-stress responses.

Harald F. Hofbauer

Harald F. Hofbauer studied Biochemistry and Molecular Biology at the University of Graz. He received his PhD in 2012 in the group of Sepp D. Kohlwein for his research on obese yeast model scenarios, which was partly performed in the laboratory of Susan A. Henry at Cornell University, Ithaca. He then continued as a PostDoc at the University of Graz in the field of lipotoxicity. In October 2014 he joined the group of Robert Ernst at Goethe University, Frankfurt, focusing on lipid-protein interactions at biological membranes.

James P. Sáenz

James P. Sáenz received his PhD from the MIT-WHOI Joint Program in Chemical Oceanography and is presently a postdoctoral fellow at the MPICBG in the group of Prof. Kai Simons. James’ research interests address the natural history and evolution of the membrane and center on understanding the evolutionary basis for lipid structural diversity. For his postdoctoral research he is studying the properties and functions of a class of bacterial ‘sterol surrogates’ called hopanoids.

Robert Ernst

Robert Ernst received his PhD from the University of Düsseldorf. In his postdoctoral phase at the Whitehead Institute for Biomedical research, he studied mechanisms of protein quality control and degradation. He then moved to the laboratory of Kai Simons to study the crosstalk of lipid and protein homeostasis. Since 2012, he has been an Emmy Noether fellow and junior professor for Molecular Membrane Biology at the Goethe University Frankfurt. In 2014 his group moved to the Buchmann Institute for Molecular Life Sciences.

Corresponding author: Robert Ernst, Institute of Biochemistry, Buchmann Institute for Molecular Life Sciences, Goethe University Frankfurt, Max-von-Laue-Str. 15, D-60438 Frankfurt/Main, Germany, e-mail:

aKristina Puth and Harald F. Hofbauer: These authors contributed equally to this work.

Received: 2015-02-18

Accepted: 2015-03-31

Published Online: 2015-04-03

Published in Print: 2015-09-01

Citation Information: Biological Chemistry, Volume 396, Issue 9-10, Pages 1043–1058, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/hsz-2015-0130.

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