Results 11 to 20 of about 882,449 (295)

SDS22 coordinates the assembly of holoenzymes from nascent protein phosphatase-1 [PDF]

Nature Communications
SDS22 forms an inactive complex with nascent protein phosphatase PP1 and Inhibitor-3. SDS22:PP1:Inhibitor-3 is a substrate for the ATPase p97/VCP, which liberates PP1 for binding to canonical regulatory subunits. The exact role of SDS22 in PP1-holoenzyme
Xinyu Cao, Madryn Lake, Gerd Van der Hoeven, Zander Claes, Javier del Pino García, Sarah Lemaire, Elora C. Greiner, Spyridoula Karamanou, Aleyde Van Eynde, Arminja N. Kettenbach, Daniel Natera de Benito, Laura Carrera García, Cristina Hernando Davalillo, Carlos Ortez, Andrés Nascimento, Roser Urreizti, Mathieu Bollen   +16 more
doaj   +2 more sources

Protein phosphatase 1 regulatory subunit 15 A promotes translation initiation and induces G2M phase arrest during cuproptosis in cancers [PDF]

Cell Death and Disease
Copper ions play a crucial role as cofactors for essential enzymes in cellular processes. However, when the intracellular concentration of copper ions exceeds the homeostatic threshold, they become toxic to cells.
Chunyu Liu, Liang Chen, Yukun Cong, Lulin Cheng, Yujun Shuai, Fang Lv, Kang Chen, Yarong Song, Yifei Xing   +8 more
doaj   +2 more sources

IRE1 phosphatase PP2Ce regulates adaptive ER stress response in the postpartum mammary gland. [PDF]

, 2013
We recently reported that the PPM1l gene encodes an endoplasmic reticulum (ER) membrane targeted protein phosphatase (named PP2Ce) with highly specific activity towards Inositol-requiring protein-1 (IRE1) and regulates the functional outcome of ER stress.
Lane, Timothy F, Lu, Gang, Ota, Asuka, Ren, Shuxun, Vondriska, Thomas M, Wang, Yibin, Zhou, Z Hong   +6 more
core   +10 more sources

Regulation of protein phosphatase-1 [PDF]

Chemistry & Biology, 2000
Reversible protein phosphorylation is a major regulatory mechanism of intracellular signal transduction. Protein phosphatase 1 (PP1) is one of four major types of serine-threonine phosphatases mediating signaling pathways, but the means by which its activity is modulated has only recently begun to come into focus.
Aggen, James B, Nairn, Angus C, Chamberlin, Richard   +2 more
openaire   +2 more sources

CBP Bromodomain Inhibition Rescues Mice From Lethal Sepsis Through Blocking HMGB1-Mediated Inflammatory Responses

Frontiers in Immunology, 2021
CREB binding protein (CBP), a transcriptional coactivator and acetyltransferase, is involved in the pathogenesis of inflammation-related diseases. High mobility group box-1 protein (HMGB1) is a critical mediator of lethal sepsis, which has prompted ...
Xiaowen Bi, Baolin Jiang, Jinyi Zhou, Xirui Fan, Xintong Yan, Juanjuan Liang, Lan Luo, Zhimin Yin   +7 more
doaj   +1 more source

Protein Phosphatase 1 Regulates Human Cytomegalovirus Protein Translation by Restraining AMPK Signaling

Frontiers in Microbiology, 2021
Human cytomegalovirus (HCMV) carries the human protein phosphatase 1 (PP1) and other human proteins important for protein translation in its tegument layer for a rapid supply upon infection.
Carmen Stecher, Sanja Marinkov, Lucia Mayr-Harting, Ana Katic, Marie-Theres Kastner, Franz J. J. Rieder-Rommer, Xionghao Lin, Sergei Nekhai, Christoph Steininger   +8 more
doaj   +1 more source

Nuclear Protein Phosphatase-1 Regulates HIV-1 Transcription [PDF]

Journal of Biological Chemistry, 2003
We recently reported that protein phosphatase 1 (PP1) dephosphorylates RNA polymerase II C-terminal repeats and regulates HIV-1 transcription in vitro. Here we provide evidence that PP1 is also required for Tat-induced HIV-1 transcription and for viral replication in cultured cells. Inhibition of PP1 by overexpression of nuclear inhibitor of PP1 (NIPP1)
Tatyana, Ammosova, Marina, Jerebtsova, Monique, Beullens, Yaroslav, Voloshin, Patricio E, Ray, Ajit, Kumar, Mathieu, Bollen, Sergei, Nekhai   +7 more
openaire   +2 more sources

Protein phosphatase-1 activates CDK9 by dephosphorylating Ser175. [PDF]

PLoS ONE, 2011
The cyclin-dependent kinase CDK9/cyclin T1 induces HIV-1 transcription by phosphorylating the carboxyterminal domain (CTD) of RNA polymerase II (RNAPII).
Tatiana Ammosova, Yuri Obukhov, Alexander Kotelkin, Denitra Breuer, Monique Beullens, Victor R Gordeuk, Mathieu Bollen, Sergei Nekhai   +7 more
doaj   +1 more source

Identification of Protein Phosphatase 1 as a Mitotic Lamin Phosphatase [PDF]

Journal of Biological Chemistry, 1997
At the onset of mitosis, the nuclear lamins are hyperphosphorylated leading to nuclear lamina disassembly, a process required for nuclear envelope breakdown and entry into mitosis. Multiple lamin kinases have been identified, including protein kinase C, that mediate mitotic lamin phosphorylation and mitotic nuclear lamina disassembly. Conversely, lamin
L J, Thompson, M, Bollen, A P, Fields
openaire   +2 more sources

The nuclear envelope protein, LAP1B, is a novel protein phosphatase 1 substrate. [PDF]

PLoS ONE, 2013
Protein phosphatase 1 (PP1) binding proteins are quintessential regulators, determining substrate specificity and defining subcellular localization and activity of the latter.
Mariana Santos, Sandra Rebelo, Paula J M Van Kleeff, Connie E Kim, William T Dauer, Margarida Fardilha, Odete A da Cruz E Silva, Edgar F da Cruz E Silva   +7 more
doaj   +1 more source