Structural highlights
Function[MIRO_DROME] Mitochondrial GTPase involved in mitochondrial trafficking. Milt and Miro form an essential protein complex that links Khc to mitochondria for light chain-independent, anterograde transport of mitochondria. Required for axonal transport to synapses within nerve terminals. Required presynaptically but not postsynaptically at neuromuscular junctions (NMJs).[1] [2] Publication Abstract from PubMedMiro is a highly conserved calcium-binding GTPase at the regulatory nexus of mitochondrial transport and autophagy. Here we present crystal structures comprising the tandem EF hand and carboxy terminal GTPase (cGTPase) domains of Drosophila Miro. The structures reveal two previously unidentified 'hidden' EF hands, each paired with a canonical EF hand. Each EF hand pair is bound to a helix that structurally mimics an EF hand ligand. A key nucleotide-sensing element and a Pink1 phosphorylation site both lie within an extensive EF hand-cGTPase interface. Our results indicate structural mechanisms for calcium, nucleotide and phosphorylation-dependent regulation of mitochondrial function by Miro. Structural coupling of the EF hand and C-terminal GTPase domains in the mitochondrial protein Miro.,Klosowiak JL, Focia PJ, Chakravarthy S, Landahl EC, Freymann DM, Rice SE EMBO Rep. 2013 Sep 27. doi: 10.1038/embor.2013.151. PMID:24071720[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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