MINPP1 prevents intracellular accumulation of the chelator inositol hexakisphosphate and is mutated in Pontocerebellar Hypoplasia

Autor: Ekin Ucuncu, Karthyayani Rajamani, Miranda S. C. Wilson, Daniel Medina-Cano, Nami Altin, Pierre David, Giulia Barcia, Nathalie Lefort, Céline Banal, Marie-Thérèse Vasilache-Dangles, Gaële Pitelet, Elsa Lorino, Nathalie Rabasse, Eric Bieth, Maha S. Zaki, Meral Topcu, Fatma Mujgan Sonmez, Damir Musaev, Valentina Stanley, Christine Bole-Feysot, Patrick Nitschké, Arnold Munnich, Nadia Bahi-Buisson, Catherine Fossoud, Fabienne Giuliano, Laurence Colleaux, Lydie Burglen, Joseph G. Gleeson, Nathalie Boddaert, Adolfo Saiardi, Vincent Cantagrel

Publikováno v: Nature Communications, Vol 11, Iss 1, Pp 1-16 (2020)

Tight regulation of inositol polyphosphate metabolism is essential for proper cell physiology. Here, the authors describe an early-onset neurodegenerative syndrome caused by loss-of-function mutations in the MINPP1 gene, characterised by intracellula

Externí odkaz: https://doaj.org/article/c86dc26738ec41afaa56ad56dca39196

Interplay between primary familial brain calcification-associated SLC20A2 and XPR1 phosphate transporters requires inositol polyphosphates for control of cellular phosphate homeostasis

Autor: Uriel López-Sánchez, Snejana Jurici, Miranda S. C. Wilson, Marc Sitbon, Valérie Courgnaud, Jean-Luc Battini, Gaël Nicolas, Xavier Ayrignac, Adolfo Saiardi, Sandrine Tury

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2020, 295 (28), pp.9366-9378. ⟨10.1074/jbc.RA119.011376⟩
Journal of Biological Chemistry, 2020, 295 (28), pp.9366-9378. ⟨10.1074/jbc.RA119.011376⟩
J Biol Chem

Solute carrier family 20 member 2 (SLC20A2) and xenotropic and polytropic retrovirus receptor 1 (XPR1) are transporters with phosphate uptake and efflux functions, respectively. Both are associated with primary familial brain calcification (PFBC), a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aba7ee9efd026ab6315bcf4365069f84
https://doi.org/10.1074/jbc.ra119.011376

The inositol hexakisphosphate kinases IP6K1 and -2 regulate human cellular phosphate homeostasis, including XPR1-mediated phosphate export

Autor: Miranda S. C. Wilson, Henning J. Jessen, Adolfo Saiardi

Publikováno v: The Journal of Biological Chemistry

Phosphate's central role in most biochemical reactions in a living organism requires carefully maintained homeostasis. Although phosphate homeostasis in mammals has long been studied at the organismal level, the intracellular mechanisms controlling p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d973073bc29dd8e6e1c5123202d76d1
https://doi.org/10.1074/jbc.ra119.007848

MINPP1 prevents intracellular accumulation of the chelator inositol hexakisphosphate and is mutated in Pontocerebellar Hypoplasia

Autor: Nathalie Rabasse, Catherine Fossoud, Nadia Bahi-Buisson, Miranda S. C. Wilson, Elsa Lorino, Celine Banal, Meral Topçu, Gaele Pitelet, Eric Bieth, Christine Bole-Feysot, Nami Altin, Vincent Cantagrel, Arnold Munnich, Marie-Therese Vasilache-Dangles, Fabienne Giuliano, Lydie Burglen, Adolfo Saiardi, Valentina Stanley, Nathalie Lefort, Giulia Barcia, Pierre David, Karthyayani Rajamani, Daniel Medina-Cano, Patrick Nitschke, Joseph G. Gleeson, Maha S. Zaki, Laurence Colleaux, Nathalie Boddaert, Fatma Mujgan Sonmez, Damir Musaev, Ekin Ucuncu

Publikováno v: Nature Communications
Nature Communications, Nature Publishing Group, 2020, 11 (1), pp.6087. ⟨10.1038/s41467-020-19919-y⟩
Nature Communications, 2020, 11 (1), pp.6087. ⟨10.1038/s41467-020-19919-y⟩
Nature Communications, Vol 11, Iss 1, Pp 1-16 (2020)

Inositol polyphosphates are vital metabolic and secondary messengers, involved in diverse cellular functions. Therefore, tight regulation of inositol polyphosphate metabolism is essential for proper cell physiology. Here, we describe an early-onset n

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::994f5bedba8a3147a651f53532ee7c82
https://doi.org/10.1038/s41467-020-19919-y

A stable immature lattice packages IP

Autor: Donna L, Mallery, Alex B, Kleinpeter, Nadine, Renner, K M Rifat, Faysal, Mariia, Novikova, Leo, Kiss, Miranda S C, Wilson, Bilal, Ahsan, Zunlong, Ke, John A G, Briggs, Adolfo, Saiardi, Till, Böcking, Eric O, Freed, Leo C, James

Publikováno v: Science Advances

HIV immature lattice stability affects capsid maturation by altering IP6 packaging.
HIV virion assembly begins with the construction of an immature lattice consisting of Gag hexamers. Upon virion release, protease-mediated Gag cleavage leads to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b7cfcc5e1fb11e52ea9f6e4d818a435c
https://pubmed.ncbi.nlm.nih.gov/33692109