Abstract:
:Miro 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.
journal_name
EMBO Repjournal_title
EMBO reportsauthors
Klosowiak JL,Focia PJ,Chakravarthy S,Landahl EC,Freymann DM,Rice SEdoi
10.1038/embor.2013.151subject
Has Abstractpub_date
2013-11-01 00:00:00pages
968-74issue
11eissn
1469-221Xissn
1469-3178pii
embor2013151journal_volume
14pub_type
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