Actin stress fiber retraction and aggresome formation is a common cellular response to actin toxins.

Biosci Biotechnol Biochem

Chemical Library Validation Team, Chemical Biology Core Facility, RIKEN Advanced Science Institute, Saitama.

Published: January 2012

F-actin-stabilizing drugs induce actin aggresome formation. In this study, we found that an actin-depolymerizing drug, latrunculin A (LatA), induced actin aggresomes. Actin stress fibers were retracted and disappeared in minutes, but a large aggresome formed in consequence of LatA treatment. Because cytochalasin D and mycalolide also induced aggresome formation, these results suggest that actin aggresome formation is a common cellular response to actin toxins.

Download full-text PDF

Source
http://dx.doi.org/10.1271/bbb.110334DOI Listing

Publication Analysis

Top Keywords

aggresome formation
16
actin stress
8
formation common
8
common cellular
8
cellular response
8
response actin
8
actin toxins
8
actin aggresome
8
actin
7
aggresome
5

Similar Publications

Ageing leads to a gradual deterioration of the organs, with the brain being particularly susceptible, often leading to neurodegeneration. This process includes well-known changes such as tau hyperphosphorylation and beta-amyloid deposition, which are commonly associated with neurodegenerative diseases but are also present in ageing. These structures are triggered by earlier cellular changes such as energy depletion and impaired protein synthesis, both of which are essential for cell function.

View Article and Find Full Text PDF

Background: Bortezomib is a standard treatment for multiple myeloma (MM), working by the accumulation of toxic misfolded proteins in cancer cells. However, a significant clinical challenge arises from the development of resistance to bortezomib in MM treatment. Aggresome, a subcellular structure enclosed within Vimentin, forms in response to proteasome inhibitors and sequesters misfolded proteins that are transported by histone deacetylase 6 (HDAC6) and Dynein for degradation via autophagy, thereby reducing bortezomib's cytotoxic effects.

View Article and Find Full Text PDF

Cells have evolved an elaborate network of folding and degradation pathways to maintain the native state of proteins. If these pathways are disrupted (e.g.

View Article and Find Full Text PDF

Proteasome inhibitors have been applied to anticancer therapy by accumulating toxic misfolded proteins. However, chemical inactivation of proteasome generates aggresome, a Vimentin cage-enclosed subcellular structure quarantining HDAC6-Dynein-transported misfolded proteins before the protein toxicants are degraded by autophagy. Hence, aggresome may attenuate proteasome inhibitor drug-induced cytotoxicity.

View Article and Find Full Text PDF

PLK2-mediated phosphorylation of SQSTM1 S349 promotes aggregation of polyubiquitinated proteins upon proteasomal dysfunction.

Autophagy

October 2024

Department of Infectious Diseases, Medical Research Institute, Zhongnan Hospital of Wuhan University, College of Life Sciences, Wuhan, China.

Dysregulation in protein homeostasis results in accumulation of protein aggregates, which are sequestered into dedicated insoluble compartments so-called inclusion bodies or aggresomes, where they are scavenged through different mechanisms to reduce proteotoxicity. The protein aggregates can be selectively scavenged by macroautophagy/autophagy called aggrephagy, which is mediated by the autophagic receptor SQSTM1. In this study, we have identified PLK2 as an important regulator of SQSTM1-mediated aggregation of polyubiquitinated proteins.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!