Specific interaction of IM30/Vipp1 with cyanobacterial and chloroplast membranes results in membrane remodeling and eventually in membrane fusion

Publication type:
Journal article
Metadata:
Autoren
  • Jennifer Heidrich
  • Adrien Thurotte
  • Dirk Schneider
DOI
10.1016/j.bbamem.2016.09.025
ISSN
0005-2736
Ausgabe der Veröffentlichung
4
Zeitschrift
Biochimica et Biophysica Acta (BBA) - Biomembranes
Sprache
en
Paginierung
537 - 549
Datum der Veröffentlichung
2017
Status
Published
Herausgeber
Elsevier BV
Herausgeber URL
http://dx.doi.org/10.1016/j.bbamem.2016.09.025
Datum der Datenerfassung
2020
Titel
Specific interaction of IM30/Vipp1 with cyanobacterial and chloroplast membranes results in membrane remodeling and eventually in membrane fusion
Ausgabe der Zeitschrift
1859

Data source: Crossref

Other metadata sources:
Abstract
The photosynthetic light reaction takes place within the thylakoid membrane system in cyanobacteria and chloroplasts. Besides its global importance, the biogenesis, maintenance and dynamics of this membrane system are still a mystery. In the last two decades, strong evidence supported the idea that these processes involve IM30, the inner membrane-associated protein of 30kDa, a protein also known as the vesicle-inducing protein in plastids 1 (Vipp1). Even though we just only begin to understand the precise physiological function of this protein, it is clear that interaction of IM30 with membranes is crucial for biogenesis of thylakoid membranes. Here we summarize and discuss forces guiding IM30-membrane interactions, as the membrane properties as well as the oligomeric state of IM30 appear to affect proper interaction of IM30 with membrane surfaces. Interaction of IM30 with membranes results in an altered membrane structure and can finally trigger fusion of adjacent membranes, when Mg<sup>2+</sup> is present. Based on recent results, we finally present a model summarizing individual steps involved in IM30-mediated membrane fusion. This article is part of a Special Issue entitled: Lipid order/lipid defects and lipid-control of protein activity edited by Dirk Schneider.
Addresses
  • Institute of Pharmacy and Biochemistry, Johannes Gutenberg-University Mainz, Johann-Joachim-Becher-Weg 30, 55128 Mainz, Germany.
Autoren
  • Jennifer Heidrich
  • Adrien Thurotte
  • Dirk Schneider
DOI
10.1016/j.bbamem.2016.09.025
eISSN
1879-2642
Externe Identifier
  • PubMed Identifier: 27693914
Funding acknowledgements
  • University of Mainz:
  • Ernst &amp; Margarete Wagemann Foundation:
  • Max Planck Institutes:
Open access
false
ISSN
0005-2736
Ausgabe der Veröffentlichung
4
Zeitschrift
Biochimica et biophysica acta. Biomembranes
Schlüsselwörter
  • Cytoskeleton
  • Thylakoids
  • Synechocystis
  • Arabidopsis
  • Cations, Divalent
  • Magnesium
  • Phospholipids
  • Bacterial Proteins
  • Membrane Proteins
  • Arabidopsis Proteins
  • Membrane Fusion
  • Photosynthesis
  • Protein Multimerization
  • Plant Cells
  • Organelle Biogenesis
Sprache
eng
Medium
Print-Electronic
Online publication date
2016
Paginierung
537 - 549
Datum der Veröffentlichung
2017
Status
Published
Datum der Datenerfassung
2016
Titel
Specific interaction of IM30/Vipp1 with cyanobacterial and chloroplast membranes results in membrane remodeling and eventually in membrane fusion.
Sub types
  • Research Support, Non-U.S. Gov't
  • Review
  • Journal Article
Ausgabe der Zeitschrift
1859

Data source: Europe PubMed Central

Abstract
The photosynthetic light reaction takes place within the thylakoid membrane system in cyanobacteria and chloroplasts. Besides its global importance, the biogenesis, maintenance and dynamics of this membrane system are still a mystery. In the last two decades, strong evidence supported the idea that these processes involve IM30, the inner membrane-associated protein of 30kDa, a protein also known as the vesicle-inducing protein in plastids 1 (Vipp1). Even though we just only begin to understand the precise physiological function of this protein, it is clear that interaction of IM30 with membranes is crucial for biogenesis of thylakoid membranes. Here we summarize and discuss forces guiding IM30-membrane interactions, as the membrane properties as well as the oligomeric state of IM30 appear to affect proper interaction of IM30 with membrane surfaces. Interaction of IM30 with membranes results in an altered membrane structure and can finally trigger fusion of adjacent membranes, when Mg2+ is present. Based on recent results, we finally present a model summarizing individual steps involved in IM30-mediated membrane fusion. This article is part of a Special Issue entitled: Lipid order/lipid defects and lipid-control of protein activity edited by Dirk Schneider.
Date of acceptance
2016
Autoren
  • Jennifer Heidrich
  • Adrien Thurotte
  • Dirk Schneider
Autoren-URL
https://www.ncbi.nlm.nih.gov/pubmed/27693914
DOI
10.1016/j.bbamem.2016.09.025
ISSN
0005-2736
Ausgabe der Veröffentlichung
4
Zeitschrift
Biochim Biophys Acta Biomembr
Schlüsselwörter
  • Chloroplasts
  • Cyanobacteria
  • IM30
  • PspA
  • Thylakoid membrane biogenesis
  • Vipp1
  • Arabidopsis
  • Arabidopsis Proteins
  • Bacterial Proteins
  • Cations, Divalent
  • Cytoskeleton
  • Magnesium
  • Membrane Fusion
  • Membrane Proteins
  • Organelle Biogenesis
  • Phospholipids
  • Photosynthesis
  • Plant Cells
  • Protein Multimerization
  • Synechocystis
  • Thylakoids
Sprache
eng
Country
Netherlands
Paginierung
537 - 549
PII
S0005-2736(16)30327-3
Datum der Veröffentlichung
2017
Status
Published
Datum, an dem der Datensatz öffentlich gemacht wurde
2017
Titel
Specific interaction of IM30/Vipp1 with cyanobacterial and chloroplast membranes results in membrane remodeling and eventually in membrane fusion.
Sub types
  • Journal Article
  • Research Support, Non-U.S. Gov't
  • Review
Ausgabe der Zeitschrift
1859

Data source: PubMed

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