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Inbar Dvilansky on Muck Rack

Inbar Dvilansky

As seen in: PLOS Biology, BioRxiv
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Articles

The human AAA-ATPase VPS4A isoform and its co-factor VTA1 have a unique function in regulating mammalian cytokinesis abscission

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By Inbar Dvilansky, Yarin Altaras, Dikla Nachmias, Nikita Kamenetsky
| PLOS Biology Verified
Loading metrics Open Access Peer-reviewed Research Article ? This is an uncorrected proof. Citation: Dvilansky I, Altaras Y, Kamenetsky N, Nachmias D, Elia N (2024) The human AAA-ATPase VPS4A isoform and its co-factor VTA1 have a unique function in regulating mammalian cytokinesis abscission. PLoS Biol 22(4): e3002327.
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Acetylation-dependent coupling between G6PD activity and apoptotic signaling

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By Fang Wu, Natali H. Muskat, Inbar Dvilansky, Omri Koren
| BioRxiv
Abstract Lysine acetylation has been discovered in thousands of non-histone human proteins, including most metabolic enzymes. Deciphering the functions of acetylation is key to understanding how metabolic cues mediate metabolic enzyme regulation and cellular signaling. Glucose-6-phosphate dehydrogenase (G6PD), the rate-limiting enzyme in the pentose phosphate pathway, is acetylated on multiple lysine residues.
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Differential role for VPS4 isoforms in cytokinetic abscission confers a regulatory function for monomeric VPS4A and VTA1 in mammalian cells

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By Inbar Dvilansky, Dikla Nachmias, Natalie Elia, Yarin Atlaras
| BioRxiv
Abstract Mutations in the human AAA-ATPase VPS4 isoform, VPS4A, cause severe Neurodevelopmental defects and Congenital Dyserythropoietic Anemia (CDA). VPS4 is a crucial component of the ESCRT system, which drives membrane remodeling in numerous cellular processes including receptor degradation, cell division and neural pruning.
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