MFN1 structures reveal nucleotide-triggered dimerization critical for mitochondrial fusion [PDF]
Mitochondria are double-membraned organelles with variable shapes influenced by metabolic conditions, developmental stage, and environmental stimuli. Their dynamic morphology is a result of regulated and balanced fusion and fission processes. Fusion is crucial for the health and physiological functions of mitochondria, including complementation of ...
Yu-Lu Cao, Jian-Xiong Feng, Yu-Jie Li
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MARCH5-mediated quality control on acetylated Mfn1 facilitates mitochondrial homeostasis and cell survival [PDF]
AbstractMitochondrial dynamics and quality control have a central role in the maintenance of cellular integrity. Mitochondrial ubiquitin ligase membrane-associated RING-CH (MARCH5) regulates mitochondrial dynamics. Here, we show that mitochondrial adaptation to stress is driven by MARCH5-dependent quality control on acetylated Mfn1. Under mitochondrial
Hyeseong Cho, Kang H, Cho H
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Identification and characterization of signal peptide of Mitofusin1 (Mfn1)
Biochemical and Biophysical Research Communications, 2019Mitofusin1 (Mfn1) mediates outer mitochondrial membrane (OMM) fusion in Opisthokonts. The uncharacterized TM comprises to two helices (namely, the TM1 and TM2) connected by an intermembrane loop. Consistent with previous studies, our results from in silico analyses show that all mitofusins lack N terminal-MTS and the TM may act an internal MTS. We have
Gopala Krishna Aradhyam
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MFN2 Plays a Distinct Role from MFN1 in Regulating Spermatogonial Differentiation [PDF]
Although mitochondrial morphology is well-known for its role in cellular homeostasis, there is surprisingly little knowledge on whether mitochondrial remodeling is required for postnatal germ cell development. In this study, we investigated the functions of MFN1 and MFN2, two GTPases in mitochondrial fusion, during early spermatogenesis.
Jingjing Zhang +2 more
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MicroRNA-19b targets Mfn1 to inhibit Mfn1-induced apoptosis in osteosarcoma cells
Accumulative evidence has confirmed that, miR-17-92, a typical polycistronic mRNA cluster, was up-regulated in various solid tumors, and play an important role in the occurrence and development progress of tumors. In our study, we detected the six members of miR-17-92 cluster in osteosarcoma cell line, finding that the expression of miR-17 and miR-19b ...
X, Li +5 more
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Neuronal injury following subarachnoid hemorrhage (SAH) has been shown to be associated with mitochondrial dysfunction and oxidative stress. βIIPKC, a subtype of protein kinase C (PKC), accumulates on the mitochondrial outer membrane and phosphorylates mitofusin 1 (Mfn1) at serine 86.
Yu-Hai Wang +2 more
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The relationship between MFN1 copy number variation and growth traits of beef cattle
Gene, 2022Copy number variation, as a kind of genetic submicroscopic structural variation, refers to the deletion or repetition of a large segment of genomic DNA, involving a segment size ranging from 50 bp to several MB. Mitochondrial fusion protein (MFN1) gene regulates the fusion of mitochondrial outer membrane in cells and maintains the dynamic needs of ...
Zhi, Yao +15 more
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MFN1-dependent alteration of mitochondrial dynamics drives hepatocellular carcinoma metastasis by glucose metabolic reprogramming [PDF]
Abstract Background Mitochondrial dynamics plays an important role in tumour progression. However, how these dynamics integrate tumour metabolism in hepatocellular carcinoma (HCC) metastasis is still unclear. Methods The mitochondrial fusion protein mitofusin-1 (MFN1 ...
Ze Zhang, Ying Zhu, Xuan Wang
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Loss of Mfn1 but not Mfn2 enhances adipogenesis
2022Abstract Objective A biallelic missense mutation in mitofusin 2 ( MFN2 ) causes multiple symmetric lipomatosis and partial lipodystrophy, implicating disruption of mitochondrial fusion or interaction with other organelles in adipocyte ...
JP Mann +13 more
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Structural basis for GTP hydrolysis and conformational change of MFN1 in mediating membrane fusion
Nature Structural & Molecular Biology, 2018Fusion of the outer mitochondrial membrane is mediated by the dynamin-like GTPase mitofusin (MFN). Here, we determined the structure of the minimal GTPase domain (MGD) of human MFN1 in complex with GDP-BeF3-. The MGD folds into a canonical GTPase fold with an associating four-helix bundle, HB1, and forms a dimer.
Liming Yan +8 more
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