Coassembly of Mgm1 isoforms requires cardiolipin and mediates mitochondrial inner membrane fusion

DeVay, Rachel M.; Domínguez-Ramírez, Lenin; Lackner, Laura L.; Hoppins, Suzanne; Stahlberg, Henning; Nunnari, Jodi

doi:10.1083/jcb.200906098

Cited by 251 publications

(234 citation statements)

References 47 publications

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“…EM images as well as two-dimensional crystallization analysis of the lattices by Fourier transformation and image processing showed a hexameric (flower-like) (26) three-fold symmetry lattice (Figs. 1F and 3, A and B, left panels), consistent with two previous studies (17,18). A structural transition in the crystalline array to a square lattice is observed by the addition of 1 mM GTP and/or its nonhydrolyzable analog GMPPCP (Fig.…”

Section: S-mgm1 Lipid-bound Oligomers Undergo a Nucleotide-dependent supporting

confidence: 78%

“…Interestingly, s-Mgm1 assembles onto liposomes independent of the presence of cardiolipin. This morphology of protein assembly is consistent both with the size of an s-Mgm1 dimer (18) and with the biological function of Mgm1 in mediating membrane fusion and possibly mitochondrial cristae maintenance. These data suggest that s-Mgm1 homo-complexes may act in trans like a zipper to tether the two membranes together to stabilize inner membrane folds and possibly facilitate fusion.…”

Section: S-mgm1 Assembles Onto the Surface Of Liposomes And Forms Promentioning

confidence: 48%

“…Negative stain was done as described previously (6,10). Two-dimensional crystals were grown and manipulated as described previously (18). Images were recorded, developed, and scanned as described previously (22).…”

Section: Methodsmentioning

confidence: 99%

“…The mechanism of action of the protein has yet to be determined, but requires two isoforms, an inner membrane-bound l-Mgm1 and an intermembrane space s-Mgm1; both isoforms contain a lipid-binding domain that is required for their in vivo function (17,18). Recent studies showed that a functional GTPase domain is only required for s-Mgm1 function, and with their differential localizations along the mitochondrial inner membrane, both isoforms are proposed to have distinct roles (19).…”

mentioning

confidence: 99%

See 3 more Smart Citations

Membrane Tethering and Nucleotide-dependent Conformational Changes Drive Mitochondrial Genome Maintenance (Mgm1) Protein-mediated Membrane Fusion

Abutbul-Ionita

Rujiviphat

Nir

et al. 2012

Journal of Biological Chemistry

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Background: Dynamin proteins shape membranes by promoting membrane curvature, fission, and fusion. Results: Cryo-EM demonstrates how the dynamin-related protein Mgm1 assembles onto and tethers membranes followed by nucleotide-dependent conformational changes. Conclusion: Mgm1 may mediate mitochondrial fusion by bridging opposing membranes and undergoing structural transitions. Significance: This study provides new mechanistic details of how dynamins may function as fusion molecules.

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Section: S-mgm1 Lipid-bound Oligomers Undergo a Nucleotide-dependent supporting

confidence: 78%

Section: S-mgm1 Assembles Onto the Surface Of Liposomes And Forms Promentioning

confidence: 48%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Membrane Tethering and Nucleotide-dependent Conformational Changes Drive Mitochondrial Genome Maintenance (Mgm1) Protein-mediated Membrane Fusion

Abutbul-Ionita

Rujiviphat

Nir

et al. 2012

Journal of Biological Chemistry

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“…Similar to Mgm1, long and short OPA1 isoforms are required for mitochondrial fusion and normal cristae structures (Song et al 2007). Cleavage of OPA1 and Mgm1 as well as the assembly of long and short isoforms is stimulated by cardiolipin, resulting in the stimulation of the GTPase activity, which promotes mitochondrial fusion (DeVay et al 2009;Ban et al 2010).…”

Section: Processing Of the Dynamin-like Gtpase Opa1mentioning

confidence: 99%

Quality Control of Mitochondrial Proteostasis

Baker

Tatsuta²,

Langer

2011

Cold Spring Harbor Perspectives in Biology

225

193

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A decline in mitochondrial activity has been associated with aging and is a hallmark of many neurological diseases. Surveillance mechanisms acting at the molecular, organellar, and cellular level monitor mitochondrial integrity and ensure the maintenance of mitochondrial proteostasis. Here we will review the central role of mitochondrial chaperones and proteases, the cytosolic ubiquitin-proteasome system, and the mitochondrial unfolded response in this interconnected quality control network, highlighting the dual function of some proteases in protein quality control within the organelle and for the regulation of mitochondrial fusion and mitophagy.

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The role of nonbilayer phospholipids in mitochondrial structure and function

2017

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Edited by Wilhelm JustMitochondrial structure and function are influenced by the unique phospholipid composition of its membranes. While mitochondria contain all the major classes of phospholipids, recent studies have highlighted specific roles of the nonbilayer-forming phospholipids phosphatidylethanolamine (PE) and cardiolipin (CL) in the assembly and activity of mitochondrial respiratory chain (MRC) complexes. The nonbilayer phospholipids are cone-shaped molecules that introduce curvature stress in the bilayer membrane and have been shown to impact mitochondrial fusion and fission. In addition to their overlapping roles in these mitochondrial processes, each nonbilayer phospholipid also plays a unique role in mitochondrial function; for example, CL is specifically required for MRC supercomplex formation. Recent discoveries of mitochondrial PE-and CL-trafficking proteins and prior knowledge of their biosynthetic pathways have provided targets for precisely manipulating nonbilayer phospholipid levels in the mitochondrial membranes in vivo. Thus, the genetic mutants of these pathways could be valuable tools in illuminating molecular functions and biophysical properties of nonbilayer phospholipids in driving mitochondrial bioenergetics and dynamics.

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Coassembly of Mgm1 isoforms requires cardiolipin and mediates mitochondrial inner membrane fusion

Abstract: The soluble and membrane-anchored isoforms of Mgm1 are only active when they work together (in trans).

Cited by 251 publications

References 47 publications

Membrane Tethering and Nucleotide-dependent Conformational Changes Drive Mitochondrial Genome Maintenance (Mgm1) Protein-mediated Membrane Fusion

Membrane Tethering and Nucleotide-dependent Conformational Changes Drive Mitochondrial Genome Maintenance (Mgm1) Protein-mediated Membrane Fusion

Quality Control of Mitochondrial Proteostasis

The role of nonbilayer phospholipids in mitochondrial structure and function

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