ArticleJournal of cell science2013
14-3-3 protein targets misfolded chaperone-associated proteins to aggresomes.
Article in Journal of cell science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed.
- Phosphorylation-dependent STAMBP drives the progression of pancreatic ductal adenocarcinoma by deubiquitinating and stabilizing BAG3.Cell death and differentiation · 2026Article
- Episodic transport of protein aggregates achieves a positive size selectivity in aggresome formation.Nature communications · 2025Article
- Disruption of BAG3-mediated BACE1 stabilization alleviates neuropathology and memory deficits in a mouse model of Alzheimer's disease.Science advances · 2025Article
- Identification of phosphatases that dephosphorylate the co-chaperone BAG3.Life science alliance · 2025Article
- Electroacupuncture alleviates Parkinson's disease by targeting HDAC/SIRT-mediated deacetylation of 14-3-3.Frontiers in aging neuroscience · 2025Article
- PARylation of 14-3-3 proteins controls the virulence of Magnaporthe oryzae.Nature communications · 2024Article
- MARK2 phosphorylates KIF13A at a 14-3-3 binding site to polarize vesicular transport of transferrin receptor within dendrites.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- BAG3 promotes proliferation and migration of arterial smooth muscle cells by regulating STAT3 phosphorylation in diabetic vascular remodeling.Cardiovascular diabetology · 2024Article
- Dysregulated Autophagy and Sarcomere Dysfunction in Patients With Heart Failure With Co-Occurrence of P63A and P380SJournal of the American Heart Association · 2023Article
- Senolytic treatment reduces oxidative protein stress in an aging male murine model of post-traumatic osteoarthritis.Aging cell · 2023Article
- Intermediate filaments associate with aggresome-like structures in proteostressed C. elegans neurons and influence large vesicle extrusions as exophers.Nature communications · 2023Article
- Article
- The Role of Small Heat Shock Proteins in Protein Misfolding Associated Motoneuron Diseases.International journal of molecular sciences · 2022Review
- The role of BAG3 in dilated cardiomyopathy and its association with Charcot-Marie-Tooth disease type 2.Acta myologica : myopathies and cardiomyopathies : official journal of the Mediterranean Society of Myology · 2022Review
- Clearance of an amyloid-like translational repressor is governed by 14-3-3 proteins.Cell reports · 2022Article
- Autophagy Modulation in Aggresome Formation: Emerging Implications and Treatments of Alzheimer's Disease.Biomedicines · 2022Review
- Valosin Containing Protein (VCP): A Multistep Regulator of Autophagy.International journal of molecular sciences · 2022Review
- Deciphering the Structure and Formation of Amyloids in Neurodegenerative Diseases With Chemical Biology Tools.Frontiers in chemistry · 2022Review
- The role of BAG3 in health and disease: A "Magic BAG of Tricks".Journal of cellular biochemistry · 2022Review
- The Hsp70-Bag3 complex modulates the phosphorylation and nuclear translocation of Hippo pathway protein Yap.Journal of cell science · 2021Article
2 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors.
Funding
Abstract
The aggresome is a key cytoplasmic organelle for sequestration and clearance of toxic protein aggregates. Although loading misfolded proteins cargos to dynein motors has been recognized as an important step in the aggresome formation process, the molecular machinery that mediates the association of cargos with the dynein motor is poorly understood. Here, we report a new aggresome-targeting pathway that involves isoforms of 14-3-3, a family of conserved regulatory proteins. 14-3-3 interacts with both the dynein-intermediate chain (DIC) and an Hsp70 co-chaperone Bcl-2-associated athanogene 3 (BAG3), thereby recruiting chaperone-associated protein cargos to dynein motors for their transport to aggresomes. This molecular cascade entails functional dimerization of 14-3-3, which we show to be crucial for the formation of aggresomes in both yeast and mammalian cells. These results suggest that 14-3-3 functions as a molecular adaptor to promote aggresomal targeting of misfolded protein aggregates and may link such complexes to inclusion bodies observed in various neurodegenerative diseases.
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