Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Stefanie Caesar"'
Autor:
Sabina Schütz, Ute Fischer, Martin Altvater, Purnima Nerurkar, Cohue Peña, Michaela Gerber, Yiming Chang, Stefanie Caesar, Olga T Schubert, Gabriel Schlenstedt, Vikram G Panse
Publikováno v:
eLife, Vol 3 (2014)
Within a single generation time a growing yeast cell imports ∼14 million ribosomal proteins (r-proteins) into the nucleus for ribosome production. After import, it is unclear how these intrinsically unstable and aggregation-prone proteins are targe
Externí odkaz:
https://doaj.org/article/3fc393b43bdf4756972fac031e350d97
Autor:
Sevde Puza, Stefanie Caesar, Chetan Poojari, Michael Jung, Ralf Seemann, Jochen S. Hub, Bianca Schrul, Jean‐Baptiste Fleury
Lipid droplets (LDs) are ubiquitous, cytoplasmic fat storage organelles that originate from the endoplasmic reticulum (ER) membrane. They are composed of a core of neutral lipids surrounded by a phospholipid monolayer. Proteins embedded into this mon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a8e1e4ce024da618270b384a3b6508b
Autor:
Lorenz Latta, François Waharte, Surayya Taranum, Stefanie Caesar, Gabriel Schlenstedt, Hanne Folz, Carlos A. Niño, Jean Salamero, Catherine Dargemont
Publikováno v:
Journal of Cell Science
Journal of Cell Science, Company of Biologists, 2019, 132 (7), pp.jcs224279. ⟨10.1242/jcs.224279⟩
Journal of Cell Science, 2019, 132 (7), pp.jcs224279. ⟨10.1242/jcs.224279⟩
Journal of Cell Science, Company of Biologists, 2019, 132 (7), pp.jcs224279. ⟨10.1242/jcs.224279⟩
Journal of Cell Science, 2019, 132 (7), pp.jcs224279. ⟨10.1242/jcs.224279⟩
The nuclear pore complex (NPC) is the major conduit for nucleocytoplasmic transport and serves as a platform for gene regulation and DNA repair. Several nucleoporins undergo ubiquitylation and SUMOylation, and these modifications play an important ro
Publikováno v:
The EMBO Journal. 31:2461-2472
The nuclear import receptor Kap114 carries transcription factors and other cargos across nuclear pores into the nucleus. Here we show that yeast Kap114 is modified by SUMO (small ubiquitin-related modifier) and that sumoylation is required for Kap114
Publikováno v:
Molecular Biology of the Cell
Activated Mpk1 MAPK regulates Swi6 nucleocytoplasmic shuttling in a bi-phasic manner. First, it recruits Swi6 to the nucleus non-catalytically by forming a nuclear Mpk1/Swi4 complex to initiate cell wall stress transcription. Then, it phosphorylates
Publikováno v:
Journal of Molecular Biology. 379:678-694
Proteins can enter the nucleus through various receptor-mediated import pathways. One class of import cargos carries a classical nuclear localization signal (cNLS) containing a short cluster of basic residues. This pathway involves importin alpha (Im
Autor:
Thomas Fries, Gabriel Schlenstedt, Kai Sohn, Christian Betz, Susanne M. Bailer, Stefanie Caesar
Publikováno v:
Journal of Biological Chemistry. 282:19292-19301
Nucleo-cytoplasmic transport of proteins is mostly mediated by specific interaction between transport receptors of the importin beta family and signal sequences present in their cargo. While several signal sequences, in particular the classical nucle
Publikováno v:
Molecular and Cellular Biology. 26:3170-3180
A characteristic feature of eukaryotic cells is that RNA synthesis and protein synthesis are separated by intracellular membranes. The compartmentalization entails transport processes between the cytoplasm and the nucleus, which take place through th
Publikováno v:
European Journal of Cell Biology. 83:511-520
Proteins are imported from the cytoplasm into the nucleus by importin beta-related transport receptors. The yeast Saccharomyces cerevisiae contains ten of these importins, but only two of them are essential. After transfer through the nuclear pore, i
Autor:
Yiming Chang, Olga T. Schubert, Sabina Schütz, Stefanie Caesar, Cohue Peña, Gabriel Schlenstedt, Vikram Govind Panse, Michaela Gerber, Purnima Nerurkar, Ute Fischer, Martin Altvater
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d11ef39ca47b249f17b77ff8a75fd7e0
https://doi.org/10.7554/elife.03473.019
https://doi.org/10.7554/elife.03473.019