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Schlattner 2018 MiP2018
Has abstract [[Image:MITOEAGLE-logo.jpg|left|100px|link
[[Image:MITOEAGLE-logo.jpg|left|100px|link=|COST Action MitoEAGLE]] Several NME proteins have NDP kinase (NDPK) activity and are thus a major source of cellular GTP. We have shown that mitochondrial NME4 localizing to the intermembrane space is using oxidatively synthesized ATP to regenerate NTPs and to stimulate respiration by the generated ADP [1]. Most importantly, NME4 is able to directly interact with and fuel the GTPase OPA1, thus supporting OPA1 functions in fusion and remodeling of the inner mitochondrial membrane MIM [2]. Both, OPA1 loss-of-function and silencing of NM23-H4, result in fusion defects that manifest in mitochondrial fragmentation [2]. We also identified a second function of NME4, which consists in intermembrane cardiolipin (CL) transfer triggered by pro-mitophagic or -apoptotic stimuli, leading to externalization of CL from the mitochondrial inner membrane to the mitochondrial surface [3,4]. There, CL acts a « eat me signal » for mitophagy or as a platform to assemble pro-apoptotic proteins. Our most recent data on HeLa cells reveal that ablating either of the two NME4 functions, phosphotransfer or CL transfer, triggers a morphogenic switch that leads to a metastasis-like cellular phenotype.
s to a metastasis-like cellular phenotype.  +
Has editor [[Plangger M]]  + , [[Kandolf G]]  +
Has title [[Image:SchlattnerU.jpg|left|90px|Uwe Schlattner]] Intramitochondrial nucleotide regeneration by NME/NDPK proteins – roles in mitochondrial dynamics, signaling and metastasis.  +
Mammal and model Human  +
Tissue and cell HeLa  +
Was published by MiPNetLab FR Grenoble Schlattner U +
Was submitted in year 2018  +
Was submitted to event MiP2018/MitoEAGLE Jurmala LV +
Was written by Schlattner U + , Tokarska-Schlattner M + , Lacombe ML + , Boissan M +
Categories Abstracts
Modification date
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07:43:00, 20 August 2018  +
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