Showing papers by "Benedikt Westermann published in 2014"
University of Freiburg1, Sapienza University of Rome2, University of Toronto3, International Institute of Minnesota4, University of California, San Diego5, University of Göttingen6, University of Washington7, Max Planck Society8, Peking University9, University of Würzburg10, University of Massachusetts Medical School11, Pohang University of Science and Technology12, Goethe University Frankfurt13, State University of New York Upstate Medical University14, Tokyo Medical and Dental University15, University of California, Los Angeles16, University of Groningen17, University of California, San Francisco18, University of Bayreuth19, University of California, Davis20
TL;DR: The mitochondrial inner membrane contains a large protein complex that functions in inner membrane organization and formation of membrane contact sites and it is proposed to unify the nomenclature and term the complex “mitochondrial contact site and cristae organizing system” and its subunits Mic10 to Mic60.
Abstract: The mitochondrial inner membrane contains a large protein complex that functions in inner membrane organization and formation of membrane contact sites The complex was variably named the mitochondrial contact site complex, mitochondrial inner membrane organizing system, mitochondrial organizing structure, or Mitofilin/Fcj1 complex To facilitate future studies, we propose to unify the nomenclature and term the complex “mitochondrial contact site and cristae organizing system” and its subunits Mic10 to Mic60
217 citations
TL;DR: It is shown that efficient mitophagy depends on mitochondrial ER tethering and affects the formation of the isolation membrane that engulfs the organelles destined for degradation, providing insights into the cellular mechanisms that govern organelle homeostasis.
180 citations
TL;DR: This review describes mitochondrial contacts with the endoplasmic reticulum, plasma membrane, and peroxisomes and highlights how mitochondrial fission, distribution, inheritance, and turnover are orchestrated by interorganellar contacts in yeast and metazoa.
99 citations
TL;DR: An unexpected but evolutionarily conserved role is reported for Arf1 and the ArfGEF GBF1 at mitochondria, involved in mitochondrial homeostasis and dynamics, independent of its role in vesicular traffic.
Abstract: The small GTPase Arf1 plays critical roles in membrane traffic by initiating the recruitment of coat proteins and by modulating the activity of lipid-modifying enzymes. Here, we report an unexpected but evolutionarily conserved role for Arf1 and the ArfGEF GBF1 at mitochondria. Loss of function of ARF-1 or GBF-1 impaired mitochondrial morphology and activity in Caenorhabditis elegans. Similarly, mitochondrial defects were observed in mammalian and yeast cells. In Saccharomyces cerevisiae, aberrant clusters of the mitofusin Fzo1 accumulated in arf1-11 mutants and were resolved by overexpression of Cdc48, an AAA-ATPase involved in ER and mitochondria-associated degradation processes. Yeast Arf1 co-fractionated with ER and mitochondrial membranes and interacted genetically with the contact site component Gem1. Furthermore, similar mitochondrial abnormalities resulted from knockdown of either GBF-1 or contact site components in worms, suggesting that the role of Arf1 in mitochondrial functioning is linked to ER–mitochondrial contacts. Thus, Arf1 is involved in mitochondrial homeostasis and dynamics, independent of its role in vesicular traffic.
76 citations
TL;DR: Past and recent advances that identified key components and cellular pathways contributing to mitochondrial inheritance in yeast are reviewed.
69 citations
TL;DR: Aim24, an inner membrane protein, by interacting with the MICOS complex plays a key role in mitochondrial architecture, composition and function.
Abstract: Structure and function of mitochondria are intimately linked. In a search for components that participate in building the elaborate architecture of this complex organelle we have identified Aim24, an inner membrane protein. Aim24 interacts with the MICOS complex that is required for the formation of crista junctions and contact sites between inner and outer membranes. Aim24 is necessary for the integrity of the MICOS complex, for normal respiratory growth and mitochondrial ultrastructure. Modification of MICOS subunits Mic12 or Mic26 by His-tags in the absence of Aim24 leads to complete loss of cristae and respiratory complexes. In addition, the level of tafazzin, a cardiolipin transacylase, is drastically reduced and the composition of cardiolipin is modified like in mutants lacking tafazzin. In conclusion, Aim24 by interacting with the MICOS complex plays a key role in mitochondrial architecture, composition and function. DOI: http://dx.doi.org/10.7554/eLife.01684.001.
66 citations
TL;DR: Yeast is used as a model organism to screen for novel components and the mitochondria-ER tether ERMES (ER-mitochondria encounter structure) is identified as a major player contributing to mitophagy and formation of mitophagosomes.
Abstract: Mitophagy is a degradative process that adapts the quantity and quality of mitochondria to the cellular needs. Mitochondria destined for degradation are marked by specific receptors that recruit the core autophagic machinery to the organellar surface. The organelle is then enclosed by a phagophore (PG) which fuses with the lysosome or vacuole where the mitochondrion is degraded. In spite of significant progress in recent years, several parts of the molecular machinery of mitophagy remain unknown. We used yeast as a model organism to screen for novel components and identified the mitochondria-ER tether ERMES (ER-mitochondria encounter structure) as a major player contributing to mitophagy and formation of mitophagosomes. Tethering of mitochondria to the ER appears to be important to supply the growing PG with lipids synthesized in the ER.
28 citations
TL;DR: A contact site between mitochondria and the lysosome-like yeast vacuole named vCLAMP is described and it is shown that it plays a role in lipid exchange, thereby linking mitochondria to the endomembrane system.
9 citations
2 citations
1 citations