keyword
MENU ▼
Read by QxMD icon Read
search

AAA ATPase

keyword
https://www.readbyqxmd.com/read/28534617/comparative-proteomics-reveals-timely-transport-into-cilia-of-regulators-or-effectors-as-a-mechanism-underlying-ciliary-disassembly
#1
Limei Wang, Lixiao Gu, Dan Meng, Qiong Wu, Haiteng Deng, Junmin Pan
Primary cilia are assembled and disassembled during cell cycle progression. During ciliary disassembly, ciliary axonemal microtubules (MTs) are depolymerized accompanied with extensive posttranslational protein modifications of ciliary proteins including protein phosphorylation, methylation and ubiquitination. These events are hypothesized to involve transport of effectors or regulators into cilia at the time of ciliary disassembly from the cell body. To prove this hypothesis and identify new proteins involved in ciliary disassembly, we analyzed disassembling flagella in Chlamydomonas using comparative proteomics with TMT labeling...
May 23, 2017: Journal of Proteome Research
https://www.readbyqxmd.com/read/28524820/chemical-structure-guided-design-of-dynapyrazoles-potent-cell-permeable-dynein-inhibitors-with-a-unique-mode-of-action
#2
Jonathan Baruch Steinman, Cristina C Santarossa, Rand M Miller, Lola S Yu, Anna S Serpinskaya, Hideki Furukawa, Sachie Morimoto, Yuta Tanaka, Mitsuyoshi Nishitani, Moriteru Asano, Ruta Zalyte, Alison E Ondrus, Alex G Johnson, Fan Ye, Maxence V Nachury, Yoshiyuki Fukase, Kazuyoshi Aso, Michael A Foley, Vladimir I Gelfand, James K Chen, Andrew P Carter, Tarun M Kapoor
Cytoplasmic dyneins are motor proteins in the AAA+ superfamily that power transport of cellular cargos towards microtubule minus-ends. Recently, ciliobrevins were reported as selective cell-permeable inhibitors of cytoplasmic dyneins. As is often true for first-in-class inhibitors, the use of ciliobrevins has been limited by low potency. Moreover, suboptimal chemical properties, such as the potential to isomerize, have hindered efforts to improve ciliobrevins. Here, we characterized the structure of ciliobrevins and designed conformationally-constrained isosteres...
May 19, 2017: ELife
https://www.readbyqxmd.com/read/28523272/structural-elements-regulating-aaa-protein-quality-control-machines
#3
REVIEW
Chiung-Wen Chang, Sukyeong Lee, Francis T F Tsai
Members of the ATPases Associated with various cellular Activities (AAA+) superfamily participate in essential and diverse cellular pathways in all kingdoms of life by harnessing the energy of ATP binding and hydrolysis to drive their biological functions. Although most AAA+ proteins share a ring-shaped architecture, AAA+ proteins have evolved distinct structural elements that are fine-tuned to their specific functions. A central question in the field is how ATP binding and hydrolysis are coupled to substrate translocation through the central channel of ring-forming AAA+ proteins...
2017: Frontiers in Molecular Biosciences
https://www.readbyqxmd.com/read/28521612/the-peroxisomal-aaa-atpase-complex-prevents-pexophagy-and-development-of-peroxisome-biogenesis-disorders
#4
Kelsey B Law, Dana Bronte-Tinkew, Erminia Di Pietro, Ann Snowden, Richard O Jones, Ann Moser, John H Brumell, Nancy Braverman, Peter K Kim
Peroxisome biogenesis disorders (PBDs) are metabolic disorders caused by the loss of peroxisomes. The majority of PBDs result from mutation in one of 3 genes that encode for the peroxisomal AAA ATPase complex (AAA-complex) required for cycling PEX5 for peroxisomal matrix protein import. Mutations in these genes are thought to result in a defect in peroxisome assembly by preventing the import of matrix proteins. However, we show here that loss of the AAA-complex does not prevent matrix protein import, but instead causes an upregulation of peroxisome degradation by macroautophagy, or pexophagy...
May 4, 2017: Autophagy
https://www.readbyqxmd.com/read/28508043/crystal-structure-of-2c-helicase-from-enterovirus-71
#5
Hongxin Guan, Juan Tian, Bo Qin, Justyna Aleksandra Wojdyla, Bei Wang, Zhendong Zhao, Meitian Wang, Sheng Cui
Enterovirus 71 (EV71) is the major pathogen responsible for outbreaks of hand, foot, and mouth disease. EV71 nonstructural protein 2C participates in many critical events throughout the virus life cycle; however, its precise role is not fully understood. Lack of a high-resolution structure made it difficult to elucidate 2C activity and prevented inhibitor development. We report the 2.5 Å-resolution crystal structure of the soluble part of EV71 2C, containing an adenosine triphosphatase (ATPase) domain, a cysteine-rich zinc finger with an unusual fold, and a carboxyl-terminal helical domain...
April 2017: Science Advances
https://www.readbyqxmd.com/read/28451587/the-interplay-of-cofactor-interactions-and-post-translational-modifications-in-the-regulation-of-the-aaa-atpase-p97
#6
REVIEW
Petra Hänzelmann, Hermann Schindelin
The hexameric type II AAA ATPase (ATPase associated with various activities) p97 (also referred to as VCP, Cdc48, and Ter94) is critically involved in a variety of cellular activities including pathways such as DNA replication and repair which both involve chromatin remodeling, and is a key player in various protein quality control pathways mediated by the ubiquitin proteasome system as well as autophagy. Correspondingly, p97 has been linked to various pathophysiological states including cancer, neurodegeneration, and premature aging...
2017: Frontiers in Molecular Biosciences
https://www.readbyqxmd.com/read/28439563/mechanism-of-vps4-hexamer-function-revealed-by-cryo-em
#7
Min Su, Emily Z Guo, Xinqiang Ding, Yan Li, Jeffrey T Tarrasch, Charles L Brooks, Zhaohui Xu, Georgios Skiniotis
Vps4 is a member of AAA(+) ATPase (adenosine triphosphatase associated with diverse cellular activities) that operates as an oligomer to disassemble ESCRT-III (endosomal sorting complex required for transport III) filaments, thereby catalyzing the final step in multiple ESCRT-dependent membrane remodeling events. We used electron cryo-microscopy to visualize oligomers of a hydrolysis-deficient Vps4 (vacuolar protein sorting-associated protein 4) mutant in the presence of adenosine 5'-triphosphate (ATP). We show that Vps4 subunits assemble into an asymmetric hexameric ring following an approximate helical path that sequentially stacks substrate-binding loops along the central pore...
April 2017: Science Advances
https://www.readbyqxmd.com/read/28416111/structural-analysis-reveals-features-of-ribosome-assembly-factor-nsa1-wdr74-important-for-localization-and-interaction-with-rix7-nvl2
#8
Yu-Hua Lo, Erin M Romes, Monica C Pillon, Mack Sobhany, Robin E Stanley
Ribosome assembly is a complex process that requires hundreds of essential assembly factors, including Rix7 (NVL2 in mammals) and Nsa1 (WDR74 in mammals). Rix7 is a type II double ring, AAA-ATPase, which is closely related to the well-known Cdc48/p97. Previous studies in Saccharomyces cerevisiae suggest that Rix7 mediates the release of Nsa1 from nucleolar pre-60S particles; however, the underlying mechanisms of this release are unknown. Through multiple structural analyses we show that S. cerevisiae Nsa1 is composed of an N-terminal seven-bladed WD40 domain followed by a lysine-rich C terminus that extends away from the WD40 domain and is required for nucleolar localization...
May 2, 2017: Structure
https://www.readbyqxmd.com/read/28400297/characterization-of-ecca3-a-cbbx-family-atpase-from-the-esx-3-secretion-pathway-of-m-tuberculosis
#9
Amit Gaur, Vijay Kumar Sharma, Sonal Shree, Niyati Rai, Ravishankar Ramachandran
EccA family proteins are conserved components of ESX secretion pathways in M. tuberculosis H37Rv. Here, we report the characterization of EccA3 (Rv0282), a CbbX family AAA (ATPases Associated with diverse cellular Activities) protein from the ESX-3 pathway that is required for in vitro growth of mycobacteria, secretion of virulence factors, and acquisition of iron and zinc. EccA3 is a thermostable ATPase with a molecular weight of ~68kDa. It exists as a dodecamer in the apo form and associates as a hexamer in the presence of ATP...
June 2017: Biochimica et Biophysica Acta
https://www.readbyqxmd.com/read/28389272/characterization-of-ciliobrevin-a-mediated-dynein-atpase-inhibition-on-flagellar-motility-of-leishmania-donovani
#10
G Srinivas Reddy, Aakash Gautam Mukhopadhyay, Chinmoy Sankar Dey
Axonemal dyneins are members of AAA+ proteins involved in force generation and are responsible for flagellar motility in eukaryotes. In this study, we characterized the effects of ciliobrevin A (CbA), a dynein ATPase inhibitor, on flagella driven motility of the protozoan parasite Leishmania donovani. Using fast-capture video microscopy, we observed that CbA decreased flagellar beat frequency of swimming parasites in a concentration-dependent manner. Beat frequency of live and reactivated L. donovani decreased by approximately 89% and 41% respectively in the presence of 250μM CbA...
April 5, 2017: Molecular and Biochemical Parasitology
https://www.readbyqxmd.com/read/28379137/structural-basis-of-protein-translocation-by-the-vps4-vta1-aaa-atpase
#11
Nicole Monroe, Han Han, Peter S Shen, Wesley I Sundquist, Christopher P Hill
Many important cellular membrane fission reactions are driven by ESCRT pathways, which culminate in disassembly of ESCRT-III polymers by the AAA ATPase Vps4. We report a 4.3 Å resolution cryo-EM structure of the active Vps4 hexamer with its cofactor Vta1, ADP·BeFx, and an ESCRT-III substrate peptide. Four Vps4 subunits form a helix whose interfaces are consistent with ATP binding, is stabilized by Vta1, and binds the substrate peptide. The fifth subunit approximately continues this helix but appears to be dissociating...
April 5, 2017: ELife
https://www.readbyqxmd.com/read/28352916/a-threonine-turnstile-defines-a-dynamic-amphiphilic-binding-motif-in-the-aaa-atpase-p97-allosteric-binding-site
#12
James C Burnett, Chaemin Lim, Brian D Peyser, Lalith P Samankumara, Marina Kovaliov, Raffaele Colombo, Stacie L Bulfer, Matthew G LaPorte, Ann R Hermone, Connor F McGrath, Michelle R Arkin, Rick Gussio, Donna M Huryn, Peter Wipf
The turnstile motion of two neighboring threonines sets up a dynamic side chain interplay that can accommodate both polar and apolar ligands in a small molecule allosteric protein binding site. A computational model based on SAR data and both X-ray and cryo-EM structures of the AAA ATPase p97 was used to analyze the effects of paired threonines at the inhibitor site. Specifically, the Thr side chain hydroxyl groups form a hydrogen bonding network that readily accommodates small, highly polar ligand substituents...
May 16, 2017: Organic & Biomolecular Chemistry
https://www.readbyqxmd.com/read/28318378/pexophagy-is-responsible-for-65-of-cases-of-peroxisome-biogenesis-disorders
#13
Taras Y Nazarko
Peroxisome biogenesis disorders (PBDs) is a group of diseases caused by mutations in one of the peroxins, proteins responsible for biogenesis of the peroxisomes. In recent years, it became clear that many peroxins (e.g., PEX3 and PEX14) play additional roles in peroxisome homeostasis (such as promoting autophagic degradation of peroxisomes or pexophagy), which are often opposite to their originally established functions in peroxisome formation and maintenance. Even more interesting, the peroxins that make up the peroxisomal AAA ATPase complex (AAA-complex) in yeast (Pex1, Pex6 and Pex15) or mammals (PEX1, PEX6, PEX26) are responsible for the downregulation of pexophagy...
February 28, 2017: Autophagy
https://www.readbyqxmd.com/read/28303975/a-conserved-inter-domain-communication-mechanism-regulates-the-atpase-activity-of-the-aaa-protein-drg1
#14
Michael Prattes, Mathias Loibl, Gertrude Zisser, Daniel Luschnig, Lisa Kappel, Ingrid Rössler, Manuela Grassegger, Altijana Hromic, Elmar Krieger, Karl Gruber, Brigitte Pertschy, Helmut Bergler
AAA-ATPases fulfil essential roles in different cellular pathways and often act in form of hexameric complexes. Interaction with pathway-specific substrate and adaptor proteins recruits them to their targets and modulates their catalytic activity. This substrate dependent regulation of ATP hydrolysis in the AAA-domains is mediated by a non-catalytic N-terminal domain. The exact mechanisms that transmit the signal from the N-domain and coordinate the individual AAA-domains in the hexameric complex are still the topic of intensive research...
March 17, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28287898/consequences-of-a-tight-squeeze-nuclear-envelope-rupture-and-repair
#15
Philipp Isermann, Jan Lammerding
Cell migration through tight spaces can induce substantial deformations of the nucleus and cause nuclear envelope (NE) rupture, resulting in uncontrolled exchange of nuclear and cytosolic proteins. These events can cause DNA damage and, in severe cases, nuclear fragmentation, challenging the integrity of the genomic material. Cells overcome NE ruptures during interphase by repairing the NE using components of the endosomal sorting complexes required for transport (ESCRT) machinery. Paralleling the molecular mechanism used during NE reformation in late mitosis, ESCRT-III subunits and the associated AAA-ATPase VPS4B are recruited to NE rupture sites and help restore NE integrity...
March 13, 2017: Nucleus
https://www.readbyqxmd.com/read/28275610/mutant-analysis-reveals-allosteric-regulation-of-clpb-disaggregase
#16
Kamila B Franke, Bernd Bukau, Axel Mogk
The members of the hexameric AAA+ disaggregase of E. coli and S. cerevisiae, ClpB, and Hsp104, cooperate with the Hsp70 chaperone system in the solubilization of aggregated proteins. Aggregate solubilization relies on a substrate threading activity of ClpB/Hsp104 fueled by ATP hydrolysis in both ATPase rings (AAA-1, AAA-2). ClpB/Hsp104 ATPase activity is controlled by the M-domains, which associate to the AAA-1 ring to downregulate ATP hydrolysis. Keeping M-domains displaced from the AAA-1 ring by association with Hsp70 increases ATPase activity due to enhanced communication between protomers...
2017: Frontiers in Molecular Biosciences
https://www.readbyqxmd.com/read/28242746/torsina-regulates-the-linc-to-moving-nuclei
#17
Daniel A Starr, Lesilee S Rose
How LINC complexes are regulated to connect nuclei to the cytoskeleton during nuclear migration is unknown. Saunders et al. (2017. J. Cell Biol. https://doi.org/10.1083/jcb.201507113) show that the AAA+ ATPase torsinA and its partner LAP1 are required for nuclear migration during fibroblast polarization by mediating the dynamics of LINC complexes.
March 6, 2017: Journal of Cell Biology
https://www.readbyqxmd.com/read/28242745/torsina-controls-tan-line-assembly-and-the-retrograde-flow-of-dorsal-perinuclear-actin-cables-during-rearward-nuclear-movement
#18
Cosmo A Saunders, Nathan J Harris, Patrick T Willey, Brian M Woolums, Yuexia Wang, Alex J McQuown, Amy Schoenhofen, Howard J Worman, William T Dauer, Gregg G Gundersen, G W Gant Luxton
The nucleus is positioned toward the rear of most migratory cells. In fibroblasts and myoblasts polarizing for migration, retrograde actin flow moves the nucleus rearward, resulting in the orientation of the centrosome in the direction of migration. In this study, we report that the nuclear envelope-localized AAA+ (ATPase associated with various cellular activities) torsinA (TA) and its activator, the inner nuclear membrane protein lamina-associated polypeptide 1 (LAP1), are required for rearward nuclear movement during centrosome orientation in migrating fibroblasts...
March 6, 2017: Journal of Cell Biology
https://www.readbyqxmd.com/read/28223493/crystal-structure-of-aquifex-aeolicus-%C3%AF-n-bound-to-promoter-dna-and-the-structure-of-%C3%AF-n-holoenzyme
#19
Elizabeth A Campbell, Shreya Kamath, Kanagalaghatta R Rajashankar, Mengyu Wu, Seth A Darst
The bacterial σ factors confer promoter specificity to the RNA polymerase (RNAP). One alternative σ factor, σ(N), is unique in its structure and functional mechanism, forming transcriptionally inactive promoter complexes that require activation by specialized AAA(+) ATPases. We report a 3.4-Å resolution X-ray crystal structure of a σ(N) fragment in complex with its cognate promoter DNA, revealing the molecular details of promoter recognition by σ(N) The structure allowed us to build and refine an improved σ(N)-holoenzyme model based on previously published 3...
March 7, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28223361/covalently-linked-hslu-hexamers-support-a-probabilistic-mechanism-that-links-atp-hydrolysis-to-protein-unfolding-and-translocation
#20
Vladimir Baytshtok, Jiejin Chen, Steven E Glynn, Andrew R Nager, Robert A Grant, Tania A Baker, Robert T Sauer
The HslUV proteolytic machine consists of HslV, a double-ring self-compartmentalized peptidase, and one or two AAA+ HslU ring hexamers that hydrolyze ATP to power the unfolding of protein substrates and their translocation into the proteolytic chamber of HslV. Here, we use genetic tethering and disulfide bonding strategies to construct HslU pseudohexamers containing mixtures of ATPase active and inactive subunits at defined positions in the hexameric ring. Genetic tethering impairs HslV binding and degradation, even for pseudohexamers with six active subunits, but disulfide-linked pseudohexamers do not have these defects, indicating that the peptide tether interferes with HslV interactions...
April 7, 2017: Journal of Biological Chemistry
keyword
keyword
27198
1
2
Fetch more papers »
Fetching more papers... Fetching...
Read by QxMD. Sign in or create an account to discover new knowledge that matter to you.
Remove bar
Read by QxMD icon Read
×

Search Tips

Use Boolean operators: AND/OR

diabetic AND foot
diabetes OR diabetic

Exclude a word using the 'minus' sign

Virchow -triad

Use Parentheses

water AND (cup OR glass)

Add an asterisk (*) at end of a word to include word stems

Neuro* will search for Neurology, Neuroscientist, Neurological, and so on

Use quotes to search for an exact phrase

"primary prevention of cancer"
(heart or cardiac or cardio*) AND arrest -"American Heart Association"