Results 91 to 100 of about 3,616 (191)

Lon degrades stable substrates slowly but with enhanced processivity, redefining the attributes of a successful AAA+ protease

open access: yesCell Reports, 2023
Summary: Lon is a widely distributed AAA+ (ATPases associated with diverse cellular activities) protease known for degrading poorly folded and damaged proteins and is often classified as a weak protein unfoldase.
Meghann R. Kasal   +6 more
doaj   +1 more source

ClpAP and ClpXP degrade proteins with tags located in the interior of the primary sequence [PDF]

open access: yesProceedings of the National Academy of Sciences, 2002
Clp/Hsp100 ATPases comprise a large family of ATP-dependent chaperones, some of which are regulatory components of two-component proteases. Substrate specificity resides in the Clp protein and the current thinking is that Clp proteins recognize motifs located near one or the other end of the substrate. We tested whether or not ClpA
Joel R, Hoskins   +3 more
openaire   +2 more sources

Dual regulatory pathways of flagellar gene expression by ClpXP protease in enterohaemorrhagic Escherichia coli

open access: yes, 2011
In enterobacteria such as Escherichia coli and Salmonella species, flagellar biogenesis is strictly dependent upon the master regulator flhDC. Here, we demonstrate that in enterohaemorrhagic E. coli (EHEC), the flagellar regulon is controlled by ClpXP, a
Ryo Kitagawa   +2 more
core   +1 more source

Proteostasis of organelles in aging and disease

open access: yesThe FEBS Journal, Volume 293, Issue 18, Page 5600-5626, September 2026.
Cells rely on regulated proteostasis mechanisms to keep their internal compartments functioning properly. When these mechanisms fail, damaged proteins accumulate, disrupting organelles, such as the nucleus, mitochondria, endoplasmic reticulum, Golgi, and lysosomes, as well as membraneless organelles, such as stress granules, processing bodies, the ...
Yara Nabawi   +5 more
wiley   +1 more source

Protein Homeostasis and Mitochondrial Quality Control in Neurodegeneration

open access: yesWIREs Mechanisms of Disease, Volume 18, Issue 4, July/August 2026.
Quality control pathways form an integrated proteostasis–mitochondrial quality control axis that maintains mitochondrial and cellular homeostasis. Failure of this coordinated network drives neuronal decline and contributes to neurodegeneration. ABSTRACT Quality control (QC) processes include a network of cellular pathways that prevent the accumulation ...
Rosa Di Lorenzo   +5 more
wiley   +1 more source

AAA+ protein unfoldases—the Moirai of the proteome

open access: yesFEBS Letters, Volume 600, Issue 10, Page 1444-1474, May 2026.
AAA+ unfoldases are essential molecular motors that power protein degradation and disaggregation. This review integrates recent cryo‐electron microscopy (cryo‐EM) structures and single‐molecule biophysical data to reconcile competing models of substrate translocation.
Stavros Azinas, Marta Carroni
wiley   +1 more source

Optimal Efficiency of ClpAP and ClpXP Chaperone-Proteases Is Achieved by Architectural Symmetry [PDF]

open access: yesStructure, 2009
A common feature of chaperone-proteases is architectural two-fold symmetry across the proteolytic cylinder. Here we investigate the role of symmetry for the function of ClpAP and ClpXP assemblies. We generated asymmetric ClpP particles in which the two rings differ in ClpA and ClpX binding capability and/or in proteolytic activity.
Maglica Z, Kolygo K, Weber-Ban E
openaire   +4 more sources

Mitochondrial Homeostasis in Pancreatic β Cell Function: Mechanisms and Therapeutic Targets for Diabetes

open access: yesJournal of Diabetes, Volume 18, Issue 5, May 2026.
This review highlights mitochondrial dysfunction as a central driver of pancreatic β cell failure in diabetes, caused by disrupted mitochondrial quality control (MQC), oxidative stress, and impaired organelle communication. Emerging therapies, such as DRAK2 inhibitors and metabolic reprogramming agents, show promise in restoring β cell function by ...
Ruihan Li   +5 more
wiley   +1 more source

Disassembly and degradation of MinD oscillator complexes by Escherichia coli ClpXP [PDF]

open access: yes, 2020
Abstract MinD is a cell division ATPase in Escherichia coli that oscillates from pole to pole and regulates the spatial position of the cell division machinery. Together with MinC and MinE, the Min system restricts assembly of the FtsZ-ring to midcell, oscillating between the ...
LaBreck, Christopher J.   +6 more
openaire   +1 more source

Identification of potential mitochondrial CLPXP protease interactors and substrates suggests its central role in energy metabolism

open access: yes, 2015
Maintenance of mitochondria is achieved by several mechanisms, including the regulation of mitochondrial proteostasis. The matrix protease CLPXP, involved in protein quality control, has been implicated in ageing and disease. However, particularly due to
Fischer, Fabian   +5 more
core   +1 more source

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