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19S regulatory particle

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https://www.readbyqxmd.com/read/28583440/proteasome-structure-and-assembly
#1
REVIEW
Lauren Budenholzer, Chin Leng Cheng, Yanjie Li, Mark Hochstrasser
The eukaryotic 26S proteasome is a large multi-subunit complex that degrades the majority of proteins in the cell under normal conditions. The 26S proteasome can be divided into two subcomplexes: the 19S regulatory particle (RP) and the 20S core particle (CP). Most substrates are first covalently modified by ubiquitin, which then directs them to the proteasome. The function of the RP is to recognize, unfold, deubiquitylate and translocate substrates into the CP, which contains the proteolytic sites of the proteasome...
June 2, 2017: Journal of Molecular Biology
https://www.readbyqxmd.com/read/28559284/the-autism-linked-ube3a-t485a-mutant-e3-ubiquitin-ligase-activates-the-wnt-%C3%AE-catenin-pathway-by-inhibiting-the-proteasome
#2
Jason J Yi, Smita R Paranjape, Matthew P Walker, Rajarshi Choudhury, Justin M Wolter, Giulia Fragola, Michael J Emanuele, Michael B Major, Mark J Zylka
UBE3A is a HECT domain E3 ubiquitin ligase whose dysfunction is linked to autism, Angelman syndrome, and cancer. Recently, we characterized a de novo autism-linked UBE3A mutant (UBE3AT485A) that disrupts phosphorylation control of UBE3A activity. Through quantitative proteomics and reporter assays, we found that the UBE3AT485A protein ubiquitinates multiple proteasome subunits, reduces proteasome subunit abundance and activity, stabilizes nuclear β-catenin, and stimulates canonical Wnt signaling more effectively than wild-type UBE3A...
May 30, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28539385/phosphatase-ublcp1-controls-proteasome-assembly
#3
Shuangwu Sun, Sisi Liu, Zhengmao Zhang, Wang Zeng, Chuang Sun, Tao Tao, Xia Lin, Xin-Hua Feng
Ubiquitin-like domain-containing C-terminal domain phosphatase 1 (UBLCP1), an FCP/SCP phosphatase family member, was identified as the first proteasome phosphatase. UBLCP1 binds to proteasome subunit Rpn1 and dephosphorylates the proteasome in vitro However, it is still unclear which proteasome subunit(s) are the bona fide substrate(s) of UBLCP1 and the precise mechanism for proteasome regulation remains elusive. Here, we show that UBLCP1 selectively binds to the 19S regulatory particle (RP) through its interaction with Rpn1, but not the 20S core particle (CP) or the 26S proteasome holoenzyme...
May 2017: Open Biology
https://www.readbyqxmd.com/read/28476333/identification-of-4-arylidene-curcumin-analogues-as-novel-proteasome-inhibitors-for-potential-anticancer-agents-targeting-19s-regulatory-particle-associated-deubiquitinase
#4
Xin Yue, Yinglin Zuo, Hongpeng Ke, Jiaming Luo, Lanlan Lou, Wenjing Qin, Youqiao Wang, Ziyi Liu, Daoyuan Chen, Haixia Sun, Weichao Zheng, Cuige Zhu, Ruimin Wang, Gesi Wen, Jun Du, Binhua Zhou, Xianzhang Bu
The proteasomal 19S regulatory particle (RP) associated deubiquitinases (DUBs) have attracted much attention owing to their potential as a therapeutic target for cancer therapy. Identification of new entities against 19S RP associated DUBs and illustration of the underlying mechanisms is crucial for discovery of novel proteasome blockers. In this study, a series of 4-arylidene curcumin analogues were identified as potent proteasome inhibitor by preferentially blocking deubiquitinase function of proteasomal 19S RP with moderate 20S CP inhibition...
August 1, 2017: Biochemical Pharmacology
https://www.readbyqxmd.com/read/28442575/structure-and-energetics-of-pairwise-interactions-between-proteasome-subunits-rpn2-rpn13-and-ubiquitin-clarify-a-substrate-recruitment-mechanism
#5
Ryan T VanderLinden, Casey W Hemmis, Tingting Yao, Howard Robinson, Christopher P Hill
The 26S proteasome is a large cellular assembly that mediates the selective degradation of proteins in the nucleus and cytosol and is an established target for anticancer therapeutics. Protein substrates are typically targeted to the proteasome through modification with a polyubiquitin chain, which can be recognized by several proteasome-associated ubiquitin receptors. One of these receptors, RPN13/ADRM1, is recruited to the proteasome through direct interaction with the large scaffolding protein RPN2 within the 19S regulatory particle...
June 9, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28396413/ubiquitinated-proteins-promote-the-association-of-proteasomes-with-the-deubiquitinating-enzyme-usp14-and-the-ubiquitin-ligase-ube3c
#6
Chueh-Ling Kuo, Alfred Lewis Goldberg
In mammalian cells, the 26S proteasomes vary in composition. In addition to the standard 28 subunits in the 20S core particle and 19 subunits in each 19S regulatory particle, a small fraction (about 10-20% in our preparations) also contains the deubiquitinating enzyme Usp14/Ubp6, which regulates proteasome activity, and the ubiquitin ligase, Ube3c/Hul5, which enhances proteasomal processivity. When degradation of ubiquitinated proteins in cells was inhibited, levels of Usp14 and Ube3c on proteasomes increased within minutes...
April 25, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28322792/molecular-chaperones-of-the-hsp70-family-assist-in-the-assembly-of-20s-proteasomes
#7
Lindsay J Hammack, Kyle Firestone, William Chang, Andrew R Kusmierczyk
The eukaryotic 26S proteasome is a large protease comprised of two major sub assemblies, the 20S proteasome, or core particle (CP), and the 19S regulatory particle (RP). Assembly of the CP and RP is assisted by an expanding list of dedicated assembly factors. For the CP, this includes Ump1 and the heterodimeric Pba1-Pba2 and Pba3-Pba4 proteins. It is not known how many additional proteins that assist in proteasome biogenesis remain to be discovered. Here, we demonstrate that two members of the Hsp70 family in yeast, Ssa1 and Ssa2, play a direct role in CP assembly...
April 29, 2017: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/27932072/a-case-for-sec61-channel-involvement-in-erad
#8
REVIEW
Karin Römisch
Proteins that misfold in the endoplasmic reticulum (ER) need to be transported back to the cytosol for degradation by proteasomes, a process known as ER-associated degradation (ERAD). The first candidate discussed as a retrograde protein transport conduit was the Sec61 channel which is responsible for secretory protein transport into the ER during biogenesis. The Sec61 channel binds the proteasome 19S regulatory particle which can extract an ERAD substrate from the ER. Nevertheless its role as a general export channel has been dismissed, and Hrd1 and Der1 have been proposed as alternatives...
December 5, 2016: Trends in Biochemical Sciences
https://www.readbyqxmd.com/read/27648923/human-telomerase-reverse-transcriptase-htert-positively-regulates-26s-proteasome-activity
#9
Eunju Im, Jong Bok Yoon, Han-Woong Lee, Kwang Chul Chung
Human telomerase reverse transcriptase (hTERT) is the catalytic subunit of telomerase, an RNA-dependent DNA polymerase that elongates telomeric DNA. hTERT displays several extra-telomeric functions that are independent of its telomere-regulatory function, including tumor progression, and neuronal cell death regulation. In this study, we evaluated these additional hTERT non-telomeric functions. We determined that hTERT interacts with several 19S and 20S proteasome subunits. The 19S regulatory particle and 20S core particle are part of 26S proteasome complex, which plays a central role in ubiquitin-dependent proteolysis...
August 2017: Journal of Cellular Physiology
https://www.readbyqxmd.com/read/27462806/an-evolutionarily-conserved-pathway-controls-proteasome-homeostasis
#10
Adrien Rousseau, Anne Bertolotti
The proteasome is essential for the selective degradation of most cellular proteins, but how cells maintain adequate amounts of proteasome is unclear. Here we show that there is an evolutionarily conserved signalling pathway controlling proteasome homeostasis. Central to this pathway is TORC1, the inhibition of which induced all known yeast 19S regulatory particle assembly-chaperones (RACs), as well as proteasome subunits. Downstream of TORC1 inhibition, the yeast mitogen-activated protein kinase, Mpk1, acts to increase the supply of RACs and proteasome subunits under challenging conditions in order to maintain proteasomal degradation and cell viability...
August 11, 2016: Nature
https://www.readbyqxmd.com/read/27430664/extracellular-proteasomes-are-deficient-in-19s-subunits-as-revealed-by-itraq-quantitative-proteomics
#11
Anna S Tsimokha, Julia J Zaykova, Andrew Bottrill, Nikolai A Barlev
Proteasome-mediated proteolysis is critical for regulation of vast majority of cellular processes. In addition to their well-documented functions in the nucleus and cytoplasm proteasomes have also been found in extracellular space. The origin and functions of these proteasomes, dubbed as circulating/plasmatic or extracellular proteasomes, are unclear. To gain insights into the molecular and functional differences between extracellular (EPs) and cellular proteasomes (CPs) we compared their subunit composition using iTRAQ-based quantitative proteomics (iTRAQ LC/MS-MS)...
April 2017: Journal of Cellular Physiology
https://www.readbyqxmd.com/read/26945516/proteomics-of-the-26s-proteasome-in-spodoptera-frugiperda-cells-infected-with-the-nucleopolyhedrovirus-acmnpv
#12
Yulia V Lyupina, Olga G Zatsepina, Marina V Serebryakova, Pavel A Erokhov, Svetlana B Abaturova, Oksana I Kravchuk, Olga V Orlova, Svetlana N Beljelarskaya, Andrey I Lavrov, Olga S Sokolova, Victor S Mikhailov
Baculoviruses are large DNA viruses that infect insect species such as Lepidoptera and are used in biotechnology for protein production and in agriculture as insecticides against crop pests. Baculoviruses require activity of host proteasomes for efficient reproduction, but how they control the cellular proteome and interact with the ubiquitin proteasome system (UPS) of infected cells remains unknown. In this report, we analyzed possible changes in the subunit composition of 26S proteasomes of the fall armyworm, Spodoptera frugiperda (Sf9), cells in the course of infection with the Autographa californica multiple nucleopolyhedrovirus (AcMNPV)...
June 2016: Biochimica et Biophysica Acta
https://www.readbyqxmd.com/read/26831523/proteomic-and-genomic-analyses-of-the-rvb1-and-rvb2-interaction-network-upon-deletion-of-r2tp-complex-components
#13
Mahadevan Lakshminarasimhan, Gina Boanca, Charles A S Banks, Gaye L Hattem, Ana E Gabriel, Brad D Groppe, Christine Smoyer, Kate E Malanowski, Allison Peak, Laurence Florens, Michael P Washburn
The highly conserved yeast R2TP complex, consisting of Rvb1, Rvb2, Pih1, and Tah1, participates in diverse cellular processes ranging from assembly of protein complexes to apoptosis. Rvb1 and Rvb2 are closely related proteins belonging to the AAA+ superfamily and are essential for cell survival. Although Rvbs have been shown to be associated with various protein complexes including the Ino80 and Swr1chromatin remodeling complexes, we performed a systematic quantitative proteomic analysis of their associated proteins and identified two additional complexes that associate with Rvb1 and Rvb2: the chaperonin-containing T-complex and the 19S regulatory particle of the proteasome complex...
March 2016: Molecular & Cellular Proteomics: MCP
https://www.readbyqxmd.com/read/26738474/structure-driven-developments-of-26s-proteasome-inhibitors
#14
REVIEW
Paweł Śledź, Wolfgang Baumeister
The 26S proteasome is a 2.5-MDa complex, and it operates at the executive end of the ubiquitin-proteasome pathway. It is a proven target for therapeutic agents for the treatment of some cancers and autoimmune diseases, and moreover, it has potential as a target of antibacterial agents. Most inhibitors, including all molecules approved for clinical use, target the 20S proteolytic core complex; its structure was determined two decades ago. Hitherto, efforts to develop inhibitors targeting the 19S regulatory particle subunits have been less successful...
2016: Annual Review of Pharmacology and Toxicology
https://www.readbyqxmd.com/read/26669444/camp-induced-phosphorylation-of-26s-proteasomes-on-rpn6-psmd11-enhances-their-activity-and-the-degradation-of-misfolded-proteins
#15
Sudarsanareddy Lokireddy, Nikolay Vadimovich Kukushkin, Alfred Lewis Goldberg
Although rates of protein degradation by the ubiquitin-proteasome pathway (UPS) are determined by their rates of ubiquitination, we show here that the proteasome's capacity to degrade ubiquitinated proteins is also tightly regulated. We studied the effects of cAMP-dependent protein kinase (PKA) on proteolysis by the UPS in several mammalian cell lines. Various agents that raise intracellular cAMP and activate PKA (activators of adenylate cyclase or inhibitors of phosphodiesterase 4) promoted degradation of short-lived (but not long-lived) cell proteins generally, model UPS substrates having different degrons, and aggregation-prone proteins associated with major neurodegenerative diseases, including mutant FUS (Fused in sarcoma), SOD1 (superoxide dismutase 1), TDP43 (TAR DNA-binding protein 43), and tau...
December 29, 2015: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/26449534/proteasome-activation-is-mediated-via-a-functional-switch-of-the-rpt6-c-terminal-tail-following-chaperone-dependent-assembly
#16
Vladyslava Sokolova, Frances Li, George Polovin, Soyeon Park
In the proteasome, the proteolytic 20S core particle (CP) associates with the 19S regulatory particle (RP) to degrade polyubiquitinated proteins. Six ATPases (Rpt1-Rpt6) of the RP form a hexameric Rpt ring and interact with the heptameric α ring (α1-α7) of the CP via the Rpt C-terminal tails individually binding to the α subunits. Importantly, the Rpt6 tail has been suggested to be crucial for RP assembly. Here, we show that the interaction of the CP and Rpt6 tail promotes a CP-Rpt3 tail interaction, and that they jointly mediate proteasome activation via opening the CP gate for substrate entry...
2015: Scientific Reports
https://www.readbyqxmd.com/read/26202105/protein-expression-of-proteasome-subunits-in-elderly-patients-with-schizophrenia
#17
Madeline R Scott, Maria D Rubio, Vahram Haroutunian, James H Meador-Woodruff
The ubiquitin proteasome system (UPS) is a major regulator of protein processing, trafficking, and degradation. While protein ubiquitination is utilized for many cellular processes, one major function of this system is to target proteins to the proteasome for degradation. In schizophrenia, studies have found UPS transcript abnormalities in both blood and brain, and we have previously reported decreased protein expression of ubiquitin-associated proteins in brain. To test whether the proteasome is similarly dysregulated, we measured the protein expression of proteasome catalytic subunits as well as essential subunits from proteasome regulatory complexes in 14 pair-matched schizophrenia and comparison subjects in superior temporal cortex...
February 2016: Neuropsychopharmacology: Official Publication of the American College of Neuropsychopharmacology
https://www.readbyqxmd.com/read/26188517/pub22-and-pub23-u-box-e3-ligases-directly-ubiquitinate-rpn6-a-26s-proteasome-lid-subunit-for-subsequent-degradation-in-arabidopsis-thaliana
#18
Seok Keun Cho, Hansol Bae, Moon Young Ryu, Seong Wook Yang, Woo TaeK Kim
Drought stress strongly affects plant growth and development, directly connected with crop yields, accordingly. However, related to the function of U-BOX E3 ligases, the underlying molecular mechanisms of desiccation stress response in plants are still largely unknown. Here we report that PUB22 and PUB23, two U-box E3 ligase homologs, tether ubiquitins to 19S proteasome regulatory particle (RP) subunit RPN6, leading to its degradation. RPN6 was identified as an interacting substrate of PUB22 by yeast two-hybrid screening, and in vitro pull-down assay confirmed that RPN6 interacts not only with PUB22, but also with PUB23...
September 4, 2015: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/26182356/base-cp-proteasome-can-serve-as-a-platform-for-stepwise-lid-formation
#19
Zanlin Yu, Nurit Livnat-Levanon, Oded Kleifeld, Wissam Mansour, Mark A Nakasone, Carlos A Castaneda, Emma K Dixon, David Fushman, Noa Reis, Elah Pick, Michael H Glickman
26S proteasome, a major regulatory protease in eukaryotes, consists of a 20S proteolytic core particle (CP) capped by a 19S regulatory particle (RP). The 19S RP is divisible into base and lid sub-complexes. Even within the lid, subunits have been demarcated into two modules: module 1 (Rpn5, Rpn6, Rpn8, Rpn9 and Rpn11), which interacts with both CP and base sub-complexes and module 2 (Rpn3, Rpn7, Rpn12 and Rpn15) that is attached mainly to module 1. We now show that suppression of RPN11 expression halted lid assembly yet enabled the base and 20S CP to pre-assemble and form a base-CP...
January 27, 2015: Bioscience Reports
https://www.readbyqxmd.com/read/26169395/binding-of-sgta-to-rpn13-selectively-modulates-protein-quality-control
#20
Pawel Leznicki, Jelena Korac-Prlic, Katarzyna Kliza, Koraljka Husnjak, Yvonne Nyathi, Ivan Dikic, Stephen High
Rpn13 is an intrinsic ubiquitin receptor of the 26S proteasome regulatory subunit that facilitates substrate capture prior to degradation. Here we show that the C-terminal region of Rpn13 binds to the tetratricopeptide repeat (TPR) domain of SGTA, a cytosolic factor implicated in the quality control of mislocalised membrane proteins (MLPs). The overexpression of SGTA results in a substantial increase in steady-state MLP levels, consistent with an effect on proteasomal degradation. However, this effect is strongly dependent upon the interaction of SGTA with the proteasomal component Rpn13...
September 1, 2015: Journal of Cell Science
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