Assembly of β-barrel proteins in the mitochondrial outer membrane

Höhr, Alexandra I. C.; Straub, Sebastian; Warscheid, Bettina; Becker, Thomas; Wiedemann, Nils

doi:10.1016/j.bbamcr.2014.10.006

Cited by 66 publications

(63 citation statements)

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“…The overexpression of these proteins reverted the globular mitochondrial morphology of mdm10 ERMES core complex, Mdm10, is a mitochondrial -barrel protein. Mdm10 is also part of another complex, sorting and assembly machinery (SAM), required for the assembly of -barrel proteins in the outer mitochondrial membrane (75,90). Because Mdm10 seems to be present in limiting amount, the availability of Mdm10 for assembling into those different complexes might play a regulatory role.…”

Section: Mitochondrial Connections Beyond Ermesmentioning

confidence: 99%

“…Mitochondria are organelles of endosymbiotic origin that, over evolution, have transferred most of their protein encoding genes into the cell host nucleus, with only a few genes still residing in the mitochondrial DNA (mtDNA) (71). Dedicated mitochondrial machineries allow for the import, folding, and assembly of the nuclear-encoded proteins required for proper mitochondrial physiology (72)(73)(74)(75). Mitochondria are also equipped with a family of carriers that facilitate the transport of small soluble molecules like amino acids, nucleotides, and vitamins across the mitochondrial inner membrane, necessary for the interdependent metabolism at both sides of the mitochondrial double membrane (76,77).…”

Section: Making Mitochondrial Membranes: the Contribution Of Er-mitocmentioning

confidence: 99%

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Lipid synthesis and membrane contact sites: a crossroads for cellular physiology

Fernández-Murray

McMaster

2016

Journal of Lipid Research

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high throughput analyses, makes this yeast a powerful organism to unveil the intricacies of this field. The yeast S. cerevisiae has played a foundational role in the field of molecular and cellular biology of lipids, including the identification of membrane contact sites (MCSs) and how they link lipid metabolism with organelle dynamics. We present advances in two topics where extensive and outstanding contributions have recently been made where their relevance transcends the yeast lipid field. We first review new information about the phosphatidic acid (PA) phosphatase, Pah1, the yeast homolog of human lipin, and its role in directing lipid flux into membrane synthesis or storage. We review the contribution of Pah1 to lipid droplet (LD) formation and its interaction with the seipin complex, Fld1/Ldb16, to regulate endoplasmic reticulum (ER)-LD contact site dynamics. Second, we recapitulate recent developments revealing MCS connections between the ER and mitochondria with other cellular compartments, and how these intersect with the maintenance of lipid homeostasis. Furthermore, we explore MCS redundancies that allow cells to cope with changing metabolic demand. PA METABOLISM CO-COORDINATES MEMBRANE AND LD SYNTHESISPA is the common precursor for the synthesis of membrane phospholipids (PLs) and the major component of The pervasive importance of lipids in cell biology has become evident. From structural roles defining cellular compartments and surfaces with specific biological properties to functional roles in signal transduction processes and modulation of regulatory networks, the involvement of lipids in varied cellular functions is well-established. Concurrently, we have gained a broad understanding about the repertoire of proteins involved in synthesis, degradation, transport, and sensing of lipids, as well as the regulatory mechanisms that interconnect lipid metabolism with other cellular processes. The amenability of Saccharomyces cerevisiae to classical approaches of molecular genetics, and toThe work on the science described in this review was supported by a Discovery Grant from the Canadian Network for Research and Innovation in Machining Technology, Natural Sciences and Engineering Research Council of Canada to C.R.M. Manuscript received 19 July 2016 and in revised form 6 August 2016. Published, JLR Papers in Press, August 12, 2016 DOI 10.1194 Lipid synthesis and membrane contact sites: a crossroads for cellular physiology Abbreviations: cER, cortical endoplasmic reticulum; ChiMERA, construct helping in mitochondria-endoplasmic reticulum association; CL, cardiolipin; DAG, diacylglycerol; EMC, endoplasmic reticulum membrane protein complex; ER, endoplasmic reticulum; ERMES, endoplasmic reticulum-mitochondria encounter structure; HOPS, homotypic fusion and vacuole protein sorting; Lam, lipid transfer protein anchored at a membrane contact site; LD, lipid droplet; Ltc, lipid transfer at contact site; LTP, lipid transfer protein; Mcp, maintenance of mitochondrial morphology 10 complementing protein; M...

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Section: Mitochondrial Connections Beyond Ermesmentioning

confidence: 99%

Section: Making Mitochondrial Membranes: the Contribution Of Er-mitocmentioning

confidence: 99%

Lipid synthesis and membrane contact sites: a crossroads for cellular physiology

Fernández-Murray

McMaster

2016

Journal of Lipid Research

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“…The core component Mia40 recognizes the precursor proteins and mediates the formation of disulfide bonds in the imported proteins. (iv) The precursors of β-barrel proteins of the outer membrane are translocated through the TOM channel to the small TIM chaperones and are inserted into the outer membrane by the sorting and assembly machinery (SAM, also termed TOB complex) (Walther and Rapaport, 2009;Höhr et al, 2015).…”

Section: Principles Of Mitochondrial Protein Importmentioning

confidence: 99%

Dynamic organization of the mitochondrial protein import machinery

Straub

Stiller

Wiedemann

et al. 2016

Biological Chemistry

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Mitochondria contain elaborate machineries for the import of precursor proteins from the cytosol. The translocase of the outer mitochondrial membrane (TOM) performs the initial import of precursor proteins and transfers the precursors to downstream translocases, including the presequence translocase and the carrier translocase of the inner membrane, the mitochondrial import and assembly machinery of the intermembrane space, and the sorting and assembly machinery of the outer membrane. Although the protein translocases can function as separate entities in vitro, recent studies revealed a close and dynamic cooperation of the protein import machineries to facilitate efficient transfer of precursor proteins in vivo. In addition, protein translocases were found to transiently interact with distinct machineries that function in the respiratory chain or in the maintenance of mitochondrial membrane architecture. Mitochondrial protein import is embedded in a regulatory network that ensures protein biogenesis, membrane dynamics, bioenergetic activity and quality control.

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Section: Introductionmentioning

confidence: 99%

“…Metaxins have been identified more recently as members of the Sorting and Assembly Machinery (SAM) (13,14) which facilitate the membrane insertion of beta-barrel proteins family which include VDAC (Höhr et al, 2015). Mtx1 has been shown to be required for the TNF-induced cell death (15) and that its deficiency led to mitochondrial anti-apoptotic phenotypes (16). Recently, we have shown that Bak interacted with Mtx2 in resting cells and with Mtx1 upon TNF treatment (6) The role and the regulation of apoptosis by the different mitochondrial receptors of the Bcl-2 family are not completely understood and it has been speculated that it could affect cell death only under specific physiological situations (17,18).…”

Section: Introductionmentioning

confidence: 99%

The phosphorylation of Metaxin 1 controls Bak activation during TNFα induced cell death

Petit

Cartron

Oliver

et al. 2017

Cellular Signalling

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International audienceThe proapoptotic protein Bak is implicated in the execution phase of apoptosis, a cell death program. Bak is essentially mitochondrial and during early steps of apoptosis undergoes conformational changes that lead to its full membrane integration in mitochondria and the subsequent liberation of pro-apoptotic mitochondrial proteins. Little is known about the partners and mechanisms implicated in the activation of Bak. We have recently shown that Bak is incorporated into a Voltage dependent anionic channel of type 2 (VDAC2)/Metaxin 1(Mtx1)/Metaxin 2 (Mtx2) multi-protein complex in both resting and dying cells. Here, we show that, after the induction of apoptosis, Bak switches from its association with Mtx2 and VDAC2 to a closer association with Mtx1. This change of partners is under the control of a tyrosine phosphorylation of Mtx1 by c-Abl

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Assembly of β-barrel proteins in the mitochondrial outer membrane

Cited by 66 publications

References 274 publications

Lipid synthesis and membrane contact sites: a crossroads for cellular physiology

Lipid synthesis and membrane contact sites: a crossroads for cellular physiology

Dynamic organization of the mitochondrial protein import machinery

The phosphorylation of Metaxin 1 controls Bak activation during TNFα induced cell death

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