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

被引：64

作者：

Klosowiak, Julian L. ^{[1
]}

Focia, Pamela J. ^{[2
]}

Chakravarthy, Srinivas ^{[3
]}

Landahl, Eric C. ^{[4
]}

Freymann, Douglas M. ^{[2
]}

Rice, Sarah E. ^{[1
]}

机构：

[1] Northwestern Univ, Dept Cell & Mol Biol, Feinberg Sch Med, Chicago, IL 60611 USA

[2] Northwestern Univ, Dept Mol Pharmacol & Biol Chem, Feinberg Sch Med, Chicago, IL 60611 USA

[3] Argonne Natl Lab, Adv Photon Source, Biophys Collaborat Access Team, Argonne, IL 60439 USA

[4] Depaul Univ, Dept Phys, Chicago, IL 60604 USA

来源：

EMBO REPORTS | 2013年 / 14卷 / 11期

关键词：

EF hand; ELM domain; GTPase; Miro; mitochondria; AXONAL-TRANSPORT; CALCIUM SENSOR; MECHANISM; SYNAPSES; MILTON; TRAFFICKING; HOMEOSTASIS; RECOVERIN; MOTILITY; PINK1;

D O I：

10.1038/embor.2013.151

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：968 / 974

页数：7

共 30 条

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