Structural coupling of the EF hand and C-terminal GTPase domains in the mitochondrial protein Miro

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 ‘hi...

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Bibliographic Details
Published in:EMBO reports 2013-11, Vol.14 (11), p.968-974
Main Authors: Klosowiak, Julian L, Focia, Pamela J, Chakravarthy, Srinivas, Landahl, Eric C, Freymann, Douglas M, Rice, Sarah E
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Autophagy
Calcium
Crystal structure
Drosophila melanogaster - metabolism
Drosophila Proteins - chemistry
Drosophila Proteins - metabolism
EF hand
EF Hand Motifs
ELM domain
EMBO40
Enzymes
GTPase
Guanosine triphosphatases
Insects
Ligands
Miro
Mitochondria
Mitochondrial Proteins - chemistry
Mitochondrial Proteins - metabolism
Models, Molecular
Molecular biology
Molecular Sequence Data
Nucleotides
Phosphorylation
Protein Structure, Tertiary
Proteins
PTEN-induced putative kinase
ras Proteins - chemistry
rho GTP-Binding Proteins - chemistry
rho GTP-Binding Proteins - metabolism
Scientific Report
Scientific Reports
Solutions
Ubiquitin-Protein Ligases - metabolism
Ubiquitination
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Summary: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. Miro is a calcium‐binding GTPase at the regulatory nexus of mitochondrial transport and autophagy. Rice and colleagues now present the first structures of Miro, revealing a novel EF hand domain arrangement and EF hand/GTPase interface, and suggest structural mechanisms for the regulation of mitochondrial function.
ISSN:1469-221X
1469-3178
DOI:10.1038/embor.2013.151