Results 51 to 60 of about 50,255 (242)

SUMO-1 promotes degradation of the polyglutamine disease protein ataxin-3

Animal Cells and Systems, 2013
Abstract Polyglutamine (polyQ) diseases are caused by the expansion of polyQ repeats in the respective gene products. Intracellular accumulation of disease proteins is a hallmark of polyQ diseases; however, whether the increased aggregation of polyQ protein is the cause of diseases is still controversial.
Na Ri Jung, Do Hee Lee
openaire   +1 more source

Proteotoxic stress reprograms the chromatin landscape of SUMO modification [PDF]

, 2015
The small ubiquitin-like modifier 2 (SUMO-2) is required for survival when cells are exposed to treatments that induce proteotoxic stress by causing the accumulation of misfolded proteins.
Anne Seifert, Geoffrey J. Barton, Pietà Schofield, Ronald T. Hay, Tanaka   +4 more
core   +3 more sources

Epstein-Barr Virus Immediate-Early Protein BZLF1 Is SUMO-1 Modified and Disrupts Promyelocytic Leukemia Bodies [PDF]

Journal of Virology, 2001
ABSTRACTAlthough the immediate-early proteins of both herpes simplex virus (HSV) and cytomegalovirus (CMV) are known to modify promyelocytic leukemia (PML) (ND10) bodies in the nucleus of the host cell, it has been unclear whether lytic infection with gamma herpesviruses induces a similar effect.
A L, Adamson, S, Kenney
openaire   +2 more sources

The Epstein-Barr virus miR-BHRF1-1 targets RNF4 during productive infection to promote the accumulation of SUMO conjugates and the release of infectious virus. [PDF]

PLoS Pathogens, 2017
Post-translational modification by the Small Ubiquitin-like Modifier (SUMO) regulates a variety of cellular functions, and is hijacked by viruses to remodel the host cell during latent and productive infection.
Jinlin Li, Simone Callegari, Maria G Masucci   +2 more
doaj   +1 more source

The Ecm11-Gmc2 complex promotes synaptonemal complex formation through assembly of transverse filaments in budding yeast [PDF]

, 2013
During meiosis, homologous chromosomes pair at close proximity to form the synaptonemal complex (SC). This association is mediated by transverse filament proteins that hold the axes of homologous chromosomes together along their entire length. Transverse
AB Zavec, AB Zavec, AJ Macqueen, AV Smith, B Kemp, B Rockmill, B Rockmill, Bilge Argunhan, BL Schneider, CE de Carvalho, CH Cheng, CM Lake, CS Eichinger, DK Bishop, E Alani, E Bolcun-Filas, F Storici, FM Lin, G Hamer, GA Brar, GV Börner, GW Hooker, H Tsubouchi, H Tsubouchi, H Tsubouchi, Hideo Tsubouchi, J Perry, JE Falk, JL Gerton, JR Hudson, L Newnham, M Lussier, M Petronczki, M Primig, M Shinohara, M Sym, M Sym, Martina Dvorackova, MN Gladstone, MS Longtine, N Hunter, Neil Humphryes, P James, PR Chua, R. Scott Hawley, S Agarwal, S Chu, S Farmer, S Schramm, SL Page, SY Chen, T Tsubouchi, T Tsubouchi, T Tsubouchi, Wing-Kit Leung, Y Costa, Yaroslav Terentyev   +56 more
core   +3 more sources

Importin-beta and CRM1 control a RANBP2 spatiotemporal switch essential for mitotic kinetochore function [PDF]

, 2017
Protein conjugation with small ubiquitin-related modifier (SUMO) is a post-translational modification that modulates protein interactions and localisation.
Damizia, Michela, DE SANTIS, RICCARDO, DE TURRIS, VALERIA, GILISTRO, EUGENIA, Lavia, Patrizia, MORONI, SARA, ROSA, ALESSANDRO, VERRICO, ANNALISA   +7 more
core   +1 more source

SUMOylation of NaV1.2 channels mediates the early response to acute hypoxia in central neurons. [PDF]

, 2016
The mechanism for the earliest response of central neurons to hypoxia-an increase in voltage-gated sodium current (INa)-has been unknown. Here, we show that hypoxia activates the Small Ubiquitin-like Modifier (SUMO) pathway in rat cerebellar granule ...
Goldstein, Steve An, Marks, Jeremy D, Plant, Leigh D   +2 more
core   +2 more sources

Nuclear pore links Fob1‐dependent rDNA damage relocation to lifespan control

FEBS Open Bio, EarlyView.
Damaged rDNA accumulates at a specific perinuclear interface that couples nucleolar escape with nuclear envelope association. Nuclear pores at this site help inhibit Fob1‐induced rDNA instability. This spatial organization of damage handling supports a functional link between nuclear architecture, rDNA stability, and replicative lifespan in yeast.
Yamato Okada, Mina Iwaki, Kyosuke Hagiri, Rei Izumi, Masahiko Harata, Chihiro Horigome   +5 more
wiley   +1 more source

Dynamic SUMO remodeling drives a series of critical events during the meiotic divisions in Caenorhabditis elegans.

PLoS Genetics, 2018
Chromosome congression and segregation in C. elegans oocytes depend on a complex of conserved proteins that forms a ring around the center of each bivalent during prometaphase; these complexes are then removed from chromosomes at anaphase onset and ...
Amanda C Davis-Roca, Nikita S Divekar, Rachel K Ng, Sarah M Wignall   +3 more
doaj   +1 more source

SUMOylation by Pias1 regulates the activity of the Hedgehog dependent Gli transcription factors. [PDF]

PLoS ONE, 2010
BACKGROUND:Hedgehog (Hh) signaling, a vital signaling pathway for the development and homeostasis of vertebrate tissues, is mediated by members of the Gli family of zinc finger transcription factors. Hh signaling increases the transcriptional activity of
Barny Cox, James Briscoe, Fausto Ulloa
doaj   +1 more source