Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Marika Miot"'
Unraveling the interplay between PKA inhibition and Cdk1 activation during oocyte meiotic maturation
Autor:
Martina Santoni, Ferdinand Meneau, Nabil Sekhsoukh, Sandrine Castella, Tran Le, Marika Miot, Enrico Maria Daldello
Publikováno v:
Cell Reports, Vol 43, Iss 2, Pp 113782- (2024)
Summary: Oocytes are arrested in prophase I. In vertebrates, meiotic resumption is triggered by hormonal stimulation that results in cAMP-dependent protein kinase (PKA) downregulation leading to Cdk1 activation. Yet the pathways connecting PKA to Cdk
Externí odkaz:
https://doaj.org/article/0a3e160d03a94c50b5766df4bfdc5767
Autor:
Tom Lemonnier, Enrico Maria Daldello, Robert Poulhe, Tran Le, Marika Miot, Laurent Lignières, Catherine Jessus, Aude Dupré
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
Mechanisms triggering meiotic divisions of oocytes remain unclear. Here, the authors report that meiosis resumption relies on the timely phosphorylation of Arpp19 protein at two distinct sites, which depends on two kinases (PKA and Gwl) and a single
Externí odkaz:
https://doaj.org/article/6154f13ed5fd440e8384d4ab8cff94e6
Publikováno v:
Frontiers in Molecular Biosciences, Vol 4 (2017)
ClpB of E. coli and yeast Hsp104 are homologous molecular chaperones and members of the AAA+ (ATPases Associated with various cellular Activities) superfamily of ATPases. They are required for thermotolerance and function in disaggregation and reacti
Externí odkaz:
https://doaj.org/article/3ad71f268e0d43a487009713ad404d6a
Autor:
Catherine Jessus, Tom Lemonnier, Marika Miot, Aude Dupré, Robert Poulhe, Enrico Maria Daldello, Laurent Lignières, Tran Le
Publikováno v:
Nature Communications
Nature Communications, Nature Publishing Group, 2021, 12, ⟨10.1038/s41467-021-22124-0⟩
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
Nature Communications, 2021, 12, ⟨10.1038/s41467-021-22124-0⟩
Nature Communications, Nature Publishing Group, 2021, 12, ⟨10.1038/s41467-021-22124-0⟩
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
Nature Communications, 2021, 12, ⟨10.1038/s41467-021-22124-0⟩
Oocytes are held in meiotic prophase for prolonged periods until hormonal signals trigger meiotic divisions. Key players of M-phase entry are the opposing Cdk1 kinase and PP2A-B55δ phosphatase. In Xenopus, the protein Arpp19, phosphorylated at serin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eea4bf66828841a0f88957de238fba54
https://hal.archives-ouvertes.fr/hal-03441642
https://hal.archives-ouvertes.fr/hal-03441642
Autor:
Tom Lemonnier, Marika Miot, Tran Le, Robert Poulhe, Aude Dupré, Enrico Maria Daldello, Catherine Jessus
Oocytes are held in meiotic prophase for prolonged periods until hormonal signals trigger meiotic divisions. Key players of M-phase entry are the opposing Cdk1 kinase and PP2A-B55δ phosphatase. InXenopus, the protein Arpp19, phosphorylated at serine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62cb5c96065fb8780569ea7db6fca65b
https://doi.org/10.1101/810549
https://doi.org/10.1101/810549
Autor:
Shannon M. Doyle, Shankar Shastry, Marika Miot, Andrea N. Kravats, Joel R. Hoskins, Yu-Hsuan Shih, George Stan, Sue Wickner
Publikováno v:
Journal of Molecular Biology. 427:312-327
The DnaK/Hsp70 chaperone system and ClpB/Hsp104 collaboratively disaggregate protein aggregates and reactivate inactive proteins. The teamwork is specific: Escherichia coli DnaK interacts with E. coli ClpB and yeast Hsp70, Ssa1, interacts with yeast
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7165f1a7722ba4301ebd659ac5cedaa6
https://doi.org/10.1016/j.jmb.2014.10.013
https://doi.org/10.1016/j.jmb.2014.10.013
Publikováno v:
Genetics. 192:185-193
Saccharomyces cerevisiae Hsp104 and Escherichia coli ClpB are Hsp100 family AAA+ chaperones that provide stress tolerance by cooperating with Hsp70 and Hsp40 to solubilize aggregated protein. Hsp104 also remodels amyloid in vitro and promotes propaga
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::704cf6554eb88a49440965dae059cc4d
https://doi.org/10.1534/genetics.112.142307
https://doi.org/10.1534/genetics.112.142307
Publikováno v:
Molecular Microbiology. 62:427-437
To examine the relationship between folding and aggregation in the periplasm of Escherichia coli, we have analysed the cellular fates of exported proteins fused to either the wild-type maltose-binding protein (MalE) or the aggregation-prone variant M
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::453f1a0fcf2b9fbd0abba241d4e6b7fa
https://doi.org/10.1111/j.1365-2958.2006.05394.x
https://doi.org/10.1111/j.1365-2958.2006.05394.x
Autor:
Danielle Johnston, Olivier Genest, Joel R. Hoskins, Daniel C. Masison, Michael Reidy, Marika Miot, Maria-Carmen Vitery, Shannon M. Doyle, Sue Wickner
Yeast Hsp104 and its bacterial homolog, ClpB, are Clp/Hsp100 molecular chaperones and AAA+ ATPases. Hsp104 and ClpB collaborate with the Hsp70 and DnaK chaperone systems, respectively, to retrieve and reactivate stress-denatured proteins from aggrega
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f60211158507c00dda1e21109ee9fbbf
https://europepmc.org/articles/PMC3084080/
https://europepmc.org/articles/PMC3084080/
Autor:
Shannon M. Doyle, Sue Wickner, Daniel C. Masison, Marika Miot, Danielle Johnston, Joel R. Hoskins, Michael Reidy
Publikováno v:
The FASEB Journal. 25
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::72e466325dad5d9e30b895b04c199ea6
https://doi.org/10.1096/fasebj.25.1_supplement.lb60
https://doi.org/10.1096/fasebj.25.1_supplement.lb60