scholarly journals Calcium Deregulation and Mitochondrial Bioenergetics in GDAP1-Related CMT Disease

2019 ◽  
Vol 20 (2) ◽  
pp. 403 ◽  
Author(s):  
Paloma González-Sánchez ◽  
Jorgina Satrústegui ◽  
Francesc Palau ◽  
Araceli del Arco
Keyword(s):  
Mitochondrial Membrane ◽  
Energy Production ◽  
Mitochondrial Dynamics ◽  
Outer Mitochondrial Membrane ◽  
Mitochondrial Network ◽  
Charcot Marie Tooth ◽  
Calcium Deregulation ◽  
Store Operated Calcium Entry ◽  
Mitochondrial Membrane Protein ◽  
Stimulation Of

The pathology of Charcot-Marie-Tooth (CMT), a disease arising from mutations in different genes, has been associated with an impairment of mitochondrial dynamics and axonal biology of mitochondria. Mutations in ganglioside-induced differentiation-associated protein 1 (GDAP1) cause several forms of CMT neuropathy, but the pathogenic mechanisms involved remain unclear. GDAP1 is an outer mitochondrial membrane protein highly expressed in neurons. It has been proposed to play a role in different aspects of mitochondrial physiology, including mitochondrial dynamics, oxidative stress processes, and mitochondrial transport along the axons. Disruption of the mitochondrial network in a neuroblastoma model of GDAP1-related CMT has been shown to decrease Ca2+ entry through the store-operated calcium entry (SOCE), which caused a failure in stimulation of mitochondrial respiration. In this review, we summarize the different functions proposed for GDAP1 and focus on the consequences for Ca2+ homeostasis and mitochondrial energy production linked to CMT disease caused by different GDAP1 mutations.

scholarly journals Genetic analysis of dTSPO , an outer mitochondrial membrane protein, reveals its functions in apoptosis, longevity, and Aβ42‐induced neurodegeneration

Aging Cell ◽  
2014 ◽  
Vol 13 (3) ◽  
pp. 507-518 ◽  
Author(s):  
Ran Lin ◽  
Alessia Angelin ◽  
Federico Da Settimo ◽  
Claudia Martini ◽  
Sabrina Taliani ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Genetic Analysis ◽  
Mitochondrial Membrane ◽  
Outer Mitochondrial Membrane ◽  
Mitochondrial Membrane Protein

scholarly journals The Outer Mitochondrial Membrane Protein mitoNEET Contains a Novel Redox-active 2Fe-2S Cluster

2007 ◽  
Vol 282 (33) ◽  
pp. 23745-23749 ◽  
Author(s):  
Sandra E. Wiley ◽  
Mark L. Paddock ◽  
Edward C. Abresch ◽  
Larry Gross ◽  
Peter van der Geer ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Mitochondrial Membrane ◽  
Outer Mitochondrial Membrane ◽  
Redox Active ◽  
Mitochondrial Membrane Protein

scholarly journals Endophilin B1 is required for the maintenance of mitochondrial morphology

2004 ◽  
Vol 166 (7) ◽  
pp. 1027-1039 ◽  
Author(s):  
Mariusz Karbowski ◽  
Seon-Yong Jeong ◽  
Richard J. Youle
Keyword(s):  
Mitochondrial Membrane ◽  
Fatty Acyl ◽  
Membrane Dynamics ◽  
Mitochondrial Morphology ◽  
Outer Mitochondrial Membrane ◽  
Mitochondrial Network ◽  
Truncated Protein ◽  
The Matrix ◽  
Membrane Compartment ◽  
Mitochondrial Distribution

We report that a fatty acyl transferase, endophilin B1, is required for maintenance of mitochondrial morphology. Down-regulation of this protein or overexpression of endophilin B1 lacking the NH2-terminal lipid-modifying domain causes striking alterations of the mitochondrial distribution and morphology. Dissociation of the outer mitochondrial membrane compartment from that of the matrix, and formation of vesicles and tubules of outer mitochondrial membrane, was also observed in both endophilin B1 knockdown cells and after overexpression of the truncated protein, indicating that endophilin B1 is required for the regulation of the outer mitochondrial membrane dynamics. We also show that endophilin B1 translocates to the mitochondria during the synchronous remodeling of the mitochondrial network that has been described to occur during apoptosis. Double knockdown of endophilin B1 and Drp1 leads to a mitochondrial phenotype identical to that of the Drp1 single knockdown, a result consistent with Drp1 acting upstream of endophilin B1 in the maintenance of morphological dynamics of mitochondria.

scholarly journals Expanding the Range of Redox Potentials of the 2Fe-2S Clusters of the Outer Mitochondrial Membrane Protein MitoNEET

2010 ◽  
Vol 98 (3) ◽  
pp. 235a
Author(s):  
John A. Zuris ◽  
Mark L. Paddock ◽  
Andrea R. Conlan ◽  
Edward C. Abresch ◽  
Rachel Nechushtai ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Mitochondrial Membrane ◽  
Outer Mitochondrial Membrane ◽  
Redox Potentials ◽  
Mitochondrial Membrane Protein

scholarly journals Crystallographic Studies of Human MitoNEET

2007 ◽  
Vol 282 (46) ◽  
pp. 33242-33246 ◽  
Author(s):  
Xiaowei Hou ◽  
Rujuan Liu ◽  
Stuart Ross ◽  
Eric J. Smart ◽  
Haining Zhu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Mitochondrial Membrane ◽  
Hydrophobic Interactions ◽  
Water Molecules ◽  
Outer Mitochondrial Membrane ◽  
Protein Fold ◽  
Close Proximity ◽  
Diabetes Drug ◽  
Mitochondrial Membrane Protein ◽  
Novel Protein

MitoNEET was identified as an outer mitochondrial membrane protein that can potentially bind the anti-diabetes drug pioglitazone. The crystal structure of the cytoplasmic mitoNEET (residues 33–108) is determined in this study. The structure presents a novel protein fold and contains a [2Fe-2S] cluster-binding domain. The [2Fe-2S] cluster is coordinated to the protein by Cys-72, Cys-74, Cys-83, and His-87 residues. This coordination is also novel compared with the traditional [2Fe-2S] cluster coordinated by four cysteines or two cysteines and two histidines. The cytoplasmic mitoNEET forms homodimers in solution and in crystal. The dimerization is mainly mediated by hydrophobic interactions as well as hydrogen bonds coordinated by two water molecules binding at the interface. His-87 residue, which plays an important role in the coordination of the [2Fe-2S] cluster, is exposed to the solvent on the dimer surface. It is proposed that mitoNEET dimer may interact with other proteins via the surface residues in close proximity to the [2Fe-2S] cluster.

scholarly journals Structural Basis for Phosphate Stabilization of the Uniquely Coordinated 2Fe-2S Cluster of the Outer Mitochondrial Membrane Protein MitoNEET.∗

2009 ◽  
Vol 96 (3) ◽  
pp. 442a-443a ◽  
Author(s):  
Christina Homer ◽  
David Yee ◽  
Herbert L. Axelrod ◽  
Aina E. Cohen ◽  
Edward C. Abresch ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Mitochondrial Membrane ◽  
Structural Basis ◽  
Outer Mitochondrial Membrane ◽  
Mitochondrial Membrane Protein
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