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Biomolecular Concepts

Editor-in-Chief: Di Cera, Enrico


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CiteScore 2018: 3.35

SCImago Journal Rank (SJR) 2018: 1.475
Source Normalized Impact per Paper (SNIP) 2018: 0.825

ICV 2017: 131.30

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Online
ISSN
1868-503X
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Volume 2, Issue 5

Issues

Membrane elongation factors in organelle maintenance: the case of peroxisome proliferation

Johannes Koch
  • Department of Biochemistry and Cell Biology, University of Vienna, Max F. Perutz Laboratories, Center of Molecular Biology, Dr. Bohr–Gasse 9, A-1030 Vienna, Austria
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Cécile Brocard
  • Department of Biochemistry and Cell Biology, University of Vienna, Max F. Perutz Laboratories, Center of Molecular Biology, Dr. Bohr–Gasse 9, A-1030 Vienna, Austria
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  • De Gruyter OnlineGoogle Scholar
Published Online: 2011-08-09 | DOI: https://doi.org/10.1515/BMC.2011.031

Abstract

Separation of metabolic pathways in organelles is critical for eukaryotic life. Accordingly, the number, morphology and function of organelles have to be maintained through processes linked with membrane remodeling events. Despite their acknowledged significance and intense study many questions remain about the molecular mechanisms by which organellar membranes proliferate. Here, using the example of peroxisome proliferation, we give an overview of how proteins elongate membranes. Subsequent membrane fission is achieved by dynamin-related proteins shared with mitochondria. We discuss basic criteria that membranes have to fulfill for these fission factors to complete the scission. Because peroxisome elongation is always associated with unequal distribution of matrix and membrane proteins, we propose peroxisomal division to be non-stochastic and asymmetric. We further show that these organelles need not be functional to carry on membrane elongation and present the most recent findings concerning members of the Pex11 protein family as membrane elongation factors. These factors, beside known proteins such as BAR-domain proteins, represent another family of proteins containing an amphipathic α-helix with membrane bending activity.

Keywords: amphipathic α-helix; DRP1/DLP1; FIS1; membrane remodeling; peroxisome proliferation; Pex11

About the article

Corresponding author


Received: 2011-05-13

Accepted: 2011-06-21

Published Online: 2011-08-09

Published in Print: 2011-10-01


Citation Information: BioMolecular Concepts, Volume 2, Issue 5, Pages 353–364, ISSN (Online) 1868-503X, ISSN (Print) 1868-5021, DOI: https://doi.org/10.1515/BMC.2011.031.

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