5gns
From Proteopedia
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/MFN1_HUMAN MFN1_HUMAN] Essential transmembrane GTPase, which mediates mitochondrial fusion. Fusion of mitochondria occurs in many cell types and constitutes an important step in mitochondria morphology, which is balanced between fusion and fission. MFN1 acts independently of the cytoskeleton. Overexpression induces the formation of mitochondrial networks.<ref>PMID:11181170</ref> <ref>PMID:12475957</ref> <ref>PMID:12759376</ref> <ref>PMID:23921378</ref> | [https://www.uniprot.org/uniprot/MFN1_HUMAN MFN1_HUMAN] Essential transmembrane GTPase, which mediates mitochondrial fusion. Fusion of mitochondria occurs in many cell types and constitutes an important step in mitochondria morphology, which is balanced between fusion and fission. MFN1 acts independently of the cytoskeleton. Overexpression induces the formation of mitochondrial networks.<ref>PMID:11181170</ref> <ref>PMID:12475957</ref> <ref>PMID:12759376</ref> <ref>PMID:23921378</ref> | ||
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| - | == Publication Abstract from PubMed == | ||
| - | Mitochondria undergo fusion and fission. The merging of outer mitochondrial membranes requires mitofusin (MFN), a dynamin-like GTPase. How exactly MFN mediates membrane fusion is poorly understood. Here, we determined crystal structures of a minimal GTPase domain (MGD) of human MFN1, including the predicted GTPase and the distal part of the C-terminal tail (CT). The structures revealed that a helix bundle (HB) formed by three helices extending from the GTPase and one extending from the CT closely attaches to the GTPase domain, resembling the configuration of bacterial dynamin-like protein. We show that the nucleotide-binding pocket is shallow and narrow, rendering weak hydrolysis and less dependence on magnesium ion, and that association of HB affects GTPase activity. MFN1 forms a dimer when GTP or GDP/BeF(3)(-), but not GDP or other analogs, is added. In addition, clustering of vesicles containing membrane-anchored MGD requires continuous GTP hydrolysis. These results suggest that MFN tethers apposing membranes, likely through nucleotide-dependent dimerization. | ||
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| - | Structures of human mitofusin 1 provide insight into mitochondrial tethering.,Qi Y, Yan L, Yu C, Guo X, Zhou X, Hu X, Huang X, Rao Z, Lou Z, Hu J J Cell Biol. 2016 Dec 5;215(5):621-629. doi: 10.1083/jcb.201609019. PMID:27920125<ref>PMID:27920125</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
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| - | <div class="pdbe-citations 5gns" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Structures of human Mitofusin 1 provide insight into mitochondrial tethering
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Categories: Homo sapiens | Large Structures | Guo X | Hu J | Hu X | Huang X | Lou Z | Qi Y | Rao Z | Yan L | Yu C | Zhou X
