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Journal Articles Science Year : 2014

Nucleoside diphosphate kinases fuel dynamin superfamily proteins with GTP for membrane remodeling

Jérome Guitton
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Abstract

Dynamin superfamily molecular motors use guanosine triphosphate (GTP) as a source of energy for membrane-remodeling events. We found that knockdown of nucleoside diphosphate kinases (NDPKs) NM23-H1/H2, which produce GTP through adenosine triphosphate (ATP)-driven conversion of guanosine diphosphate (GDP), inhibited dynamin-mediated endocytosis. NM23-H1/H2 localized at clathrin-coated pits and interacted with the proline-rich domain of dynamin. In vitro, NM23-H1/H2 were recruited to dynamin-induced tubules, stimulated GTP-loading on dynamin, and triggered fission in the presence of ATP and GDP. NM23-H4, a mitochondria-specific NDPK, colocalized with mitochondrial dynamin-like OPA1 involved in mitochondria inner membrane fusion and increased GTP-loading on OPA1. Like OPA1 loss of function, silencing of NM23-H4 but not NM23-H1/H2 resulted in mitochondrial fragmentation, reflecting fusion defects. Thus, NDPKs interact with and provide GTP to dynamins, allowing these motor proteins to work with high thermodynamic efficiency.
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Dates and versions

hal-01870066 , version 1 (05-12-2023)

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Mathieu Boissan, Guillaume Montagnac, Qinfang Shen, Lorena Griparic, Jérome Guitton, et al.. Nucleoside diphosphate kinases fuel dynamin superfamily proteins with GTP for membrane remodeling. Science, 2014, 344 (6191), pp.1510 - 1515. ⟨10.1126/science.1253768⟩. ⟨hal-01870066⟩
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