Results 51 to 60 of about 234,152 (246)

The AAA+ ATPase Msp1 is a processive protein translocase with robust unfoldase activity

Proceedings of the National Academy of Sciences of the United States of America, 2020
Significance The AAA+ ATPase Msp1 has previously been shown to function in the quality control of tail-anchored proteins at the mitochondrial and peroxisomal membranes, yet its detailed mechanisms of substrate processing have remained unknown.
D. Castanzo, B. LaFrance, Andreas Martin
semanticscholar   +1 more source

LRRK2 phosphorylates pre-synaptic N-ethylmaleimide sensitive fusion (NSF) protein enhancing its ATPase activity and SNARE complex disassembling rate [PDF]

, 2016
Background Lrrk2, a gene linked to Parkinson\u2019s disease, encodes a large scaffolding protein with kinase and GTPase activities implicated in vesicle and cytoskeletal-related processes.
Arrigoni, Giorgio, Belluzzi, Elisa, Beltramini, Mariano, Bubacco, Luigi, Carrion, Maria Per\ue8z, Cirnaru, Maria Daniela, Civiero, Laura, Cogo, Susanna, Franchin, Cinzia, Gonnelli, Adriano, Greggio, Elisa, Marte, Antonella, Onofri, Franco, Piccoli, Giovanni, Plotegher, Nicoletta, Russo, Isabella   +15 more
core   +5 more sources

The CryoEM structure of the Saccharomyces cerevisiae ribosome maturation factor Rea1

eLife, 2018
The biogenesis of 60S ribosomal subunits is initiated in the nucleus where rRNAs and proteins form pre-60S particles. These pre-60S particles mature by transiently interacting with various assembly factors.
Piotr Sosnowski, Linas Urnavicius, Andreas Boland, Robert Fagiewicz, Johan Busselez, Gabor Papai, Helgo Schmidt   +6 more
doaj   +1 more source

A Ycf2-FtsHi Heteromeric AAA-ATPase Complex Is Required for Chloroplast Protein Import[OPEN]

The Plant Cell, 2018
A protease-originated membrane-bound AAA-ATPase is involved in preprotein translocation across the inner envelope membrane of chloroplasts as an essential import motor.
S. Kikuchi, Y. Asakura, Midori Imai, Y. Nakahira, Yoshiko Kotani, Y. Hashiguchi, Y. Nakai, K. Takafuji, Jocelyn Bédard, Yoshino Hirabayashi-Ishioka, H. Mori, T. Shiina, M. Nakai   +12 more
semanticscholar   +1 more source

Proteasomal AAA-ATPases: Structure and function

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2012
The 26S proteasome is a chambered protease in which the majority of selective cellular protein degradation takes place. Throughout evolution, access of protein substrates to chambered proteases is restricted and depends on AAA-ATPases. Mechanical force generated through cycles of ATP binding and hydrolysis is used to unfold substrates, open the gated ...
Bar-Nun, Shoshana, Glickman, Michael H.
openaire   +2 more sources

AAA⁺ superfamily ATPases: common structure–diverse function [PDF]

Genes to Cells, 2001
The AAA+ superfamily of ATPases, which contain a homologous ATPase module, are found in all kingdoms of living organisms where they participate in diverse cellular processes including membrane fusion, proteolysis and DNA replication. Recent structural studies have revealed that they usually form ring‐shaped oligomers, which are crucial for their ATPase
T, Ogura, A J, Wilkinson
openaire   +2 more sources

The proteasome cap RPT5/Rpt5p subunit prevents aggregation of unfolded ricin A chain [PDF]

, 2013
The plant cytotoxin ricin enters mammalian cells by receptor-mediated endocytosis, undergoing retrograde transport to the endoplasmic reticulum (ER) where its catalytic A chain (RTA) is reductively separated from the holotoxin to enter the cytosol and ...
Afshar, Allen, Argent, Bays, Bellisola, Blum, Braun, Brodsky, Carvalho, Cascio, Craiu, David M. Roberts, Deeks, Elkabetz, Endo, Fiani, Fleming, Fu, Gallastegui, Giodini, Groll, Hartley, Hazes, Heiligenstein, Heinemeyer, Hendil, Holmberg, Hudson, Husnjak, J. Michael Lord, Jarosch, Jin, Jonathan P. Cook, Kohler, Lam, Li, Li, Lipson, Lundgren, Lynne M. Roberts, May, Mayerhofer, Nishi Vasisht, Paola Pietroni, Rabinovich, Rasmus Hartmann-Petersen, Redmann, Robert A. Spooner, Rubin, Sandvig, Schreiner, Sokolowska, Spooner, Spooner, Spooner, Spooner, Strickland, Surjit, Unno, van Nocker, Wesche, Ye   +61 more
core   +2 more sources

The emerging role of E3 ubiquitin ligase RNF213 as an antimicrobial host determinant

Frontiers in Cellular and Infection Microbiology, 2023
Ring finger protein 213 (RNF213) is a large E3 ubiquitin ligase with a molecular weight of 591 kDa that is associated with moyamoya disease, a rare cerebrovascular disease. It is located in the cytosol and perinuclear space.
Yulu Zhang, Yulu Zhang, Yulu Zhang, Yupei Yuan, Yupei Yuan, Lu Jiang, Lu Jiang, Yihan Liu, Yihan Liu, Leiliang Zhang, Leiliang Zhang, Leiliang Zhang   +11 more
doaj   +1 more source

Structural mechanism for nucleotide-driven remodeling of the AAA-ATPase unfoldase in the activated human 26S proteasome

Nature Communications, 2018
The proteasome is a sophisticated ATP-dependent molecular machine responsible for protein degradation in all known eukaryotic cells. It remains elusive how conformational changes of the AAA-ATPase unfoldase in the regulatory particle (RP) control the ...
R. Shalloo, S. Dann, J-N Gruse, C. Underwood, A. Antoine, C. Arran, M. Backhouse, C. Baird, M. Balcazar, N. Bourgeois, J. Cardarelli, P. Hatfield, J. Kang, Karl Krushelnick, S. Mangles, C. Murphy, N. Lu, J. Osterhoff, K. Põder, P. Rajeev, C. Ridgers, S. Rozario, M. Selwood, A. Shahani, D. Symes, A. Thomas, C. Thornton, Z. Najmudin, M. Streeter   +28 more
semanticscholar   +1 more source

Diverged composition and regulation of the Trypanosoma brucei origin recognition complex that mediates DNA replication initiation [PDF]

, 2016
Initiation of DNA replication depends upon recognition of genomic sites, termed origins, by AAA+ ATPases. In prokaryotes a single factor binds each origin, whereas in eukaryotes this role is played by a six-protein origin recognition complex (ORC).
Damasceno, Jeziel D., Lemgruber Soares, Leandro, Marcello, Lucio, Marques, Catarina A., McCulloch, Richard, Paape, Daniel, Scott, Alan, Tiengwe, Calvin   +7 more
core   +3 more sources