HSPA9/Mortalin mediates axo-protection and modulates mitochondrial dynamics in neurons

Autor: Ferré, Cécile, Thouard, Anne, Bétourné, Alexandre, Le Dorze, Anne-Louise, Belenguer, Pascale, Miquel, Marie-Christine, Peyrin, Jean-Michel, Gonzalez-Dunia, Daniel, Szelechowski, Marion

Publikováno v: Scientific Reports
Scientific Reports, Nature Publishing Group, 2021, 11 (1), ⟨10.1038/s41598-021-97162-1⟩
Scientific Reports, Vol 11, Iss 1, Pp 1-12 (2021)
Scientific Reports, 2021, 11 (1), pp.17705. ⟨10.1038/s41598-021-97162-1⟩
Scientific Reports, Nature Publishing Group, 2021, 11 (1), pp.17705. ⟨10.1038/s41598-021-97162-1⟩

International audience; Abstract Mortalin is a mitochondrial chaperone protein involved in quality control of proteins imported into the mitochondrial matrix, which was recently described as a sensor of neuronal stress. Mortalin is down-regulated in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::5bdfacbb75cb9f9458677eb3bc34d63f
https://hal.archives-ouvertes.fr/hal-03424565

Proteasomal degradation of NOD2 by NLRP12 in monocytes promotes bacterial tolerance and colonization by enteropathogens

Autor: Normand, Sylvain, Waldschmitt, Nadine, Neerincx, Andreas, Martinez-Torres, Ruben Julio, Chauvin, Camille, Couturier-Maillard, Aurelie, Boulard, Olivier, Cobret, Laetitia, Awad, Fawaz, Huot, Ludovic, Ribeiro-Ribeiro, Andre, Lautz, Katja, Ruez, Richard, Delacre, Myriam, Bondu, Clovis, Guilliams, Martin, Scott, Charlotte, Segal, Anthony, Amselem, Serge, Hot, David, Karabina, Sonia, Bohn, Erwin, Ryffel, Bernhard, Poulin, Lionel F, Kufer, Thomas A, Chamaillard, Mathias

Publikováno v: Nature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
Nature Communications
Nature Communications, 2018, 9, pp.5338. ⟨10.1038/s41467-018-07750-5⟩
Nature Communications, Nature Publishing Group, 2018, 9 (1), ⟨10.1038/s41467-018-07750-5⟩
Nature Communications, Nature Publishing Group, 2018, 9, pp.5338. ⟨10.1038/s41467-018-07750-5⟩
NATURE COMMUNICATIONS

Mutations in the nucleotide-binding oligomerization domain protein 12 (NLRP12) cause recurrent episodes of serosal inflammation. Here we show that NLRP12 efficiently sequesters HSP90 and promotes K48-linked ubiquitination and degradation of NOD2 in r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::e50944fc482415c00f8748ca8a1bb1ad
http://link.springer.com/article/10.1038/s41467-018-07750-5

Chaperone-Mediated Autophagy Markers LAMP2A and HSC70 Are Independent Adverse Prognostic Markers in Primary Resected Squamous Cell Carcinomas of the Lung

Autor: Mario P. Tschan, Anna M. Schläfli, Sabina Berezowska, Ralph A. Schmid, Tereza Losmanová, Magali Humbert, Félice A. Janser, Rupert Langer, Christina Neppl, Igor Tokarchuk

Publikováno v: Oxidative Medicine and Cellular Longevity
Losmanová, Tereza; Janser, Félice A.; Humbert, Magali; Tokarchuk, Igor; Schläfli, Anna M.; Neppl, Christina; Schmid, Ralph; Tschan, Mario P.; Langer, Rupert; Berezowska, Sabina (2020). Chaperone-Mediated Autophagy Markers LAMP2A and HSC70 Are Independent Adverse Prognostic Markers in Primary Resected Squamous Cell Carcinomas of the Lung. Oxidative medicine and cellular longevity, 2020, p. 8506572. Hindawi 10.1155/2020/8506572
Oxidative medicine and cellular longevity, vol. 2020, pp. 8506572
Oxidative Medicine and Cellular Longevity, Vol 2020 (2020)

LAMP2A and HSC70 are crucial players in chaperone-mediated autophagy (CMA), a targeted, lysosome-dependent protein degradation pathway. Elevated LAMP2A levels, indicative of increased CMA activity, are observed in several malignancies, and CMA downre

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1f7c444a62405c2d5a9f291e5553505
http://europepmc.org/articles/PMC7527932

Non-enzymatic cleavage of Hsp90 by oxidative stress leads to actin aggregate formation: A novel gain-of-function mechanism

Autor: Tilman Grune, Henrique Almeida, Raquel Fernando, José Pedro Castro, Sandra Reeg, Walter Meinl

Publikováno v: Redox Biology, Vol 21, Iss, Pp-(2019)
Redox Biology

Aging is accompanied by the accumulation of oxidized proteins. To remove them, cells employ the proteasomal and autophagy-lysosomal systems; however, if the clearance rate is inferior to its formation, protein aggregates form as a hallmark of proteos

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b699b02bf2aeb0a16d74f0d4b19b2ba
http://www.sciencedirect.com/science/article/pii/S2213231718312369

Involvement of Hsp90 and cyclophilins in intoxication by AIP56, a metalloprotease toxin from Photobacterium damselae subsp. piscicida

Autor: Johnny Lisboa, Inês S Rodrigues, Pedro Oliveira, Ana do Vale, Liliana M. G. Pereira, Cassilda Pereira, Nuno M. S. dos Santos

Publikováno v: Scientific Reports
Scientific Reports, Vol 9, Iss 1, Pp 1-13 (2019)

AIP56 (apoptosis inducing protein of 56 kDa) is a key virulence factor secreted by virulent strains of Photobacterium damselae subsp. piscicida (Phdp), a Gram-negative bacterium that causes septicemic infections in several warm water marine fish spec

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e77e6bbf4cc0b51166a777cec805450
https://hdl.handle.net/10216/136355