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14-3-3 and aggresome formation

Title: 14-3-3 and aggresome formation: implications in neurodegenerative diseases.
Name(s): Jia, Baohui, author
Wu, Yuying, author
Zhou, Yi, author
Type of Resource: text
Genre: Journal Article
Date Issued: 2014-03-01
Physical Form: computer
online resource
Extent: 1 online resource
Language(s): English
Abstract/Description: Protein misfolding and aggregation underlie the pathogenesis of many neurodegenerative diseases. In addition to chaperone-mediated refolding and proteasomal degradation, the aggresome-macroautophagy pathway has emerged as another defense mechanism for sequestration and clearance of toxic protein aggregates in cells. Previously, the 14-3-3 proteins were shown to be indispensable for the formation of aggresomes induced by mutant huntingtin proteins. In a recent study, we have determined that 14-3-3 functions as a molecular adaptor to recruit chaperone-associated misfolded proteins to dynein motors for transport to aggresomes. This molecular complex involves a dimeric binding of 14-3-3 to both the dynein-intermediate chain (DIC) and an Hsp70 co-chaperone Bcl-2-associated athanogene 3 (BAG3). As 14-3-3 has been implicated in various neurodegenerative diseases, our findings may provide mechanistic insights into its role in managing misfolded protein stress during the process of neurodegeneration.
Identifier: FSU_pmch_24549097 (IID), PMC4189886 (PMCID), 24549097 (RID), 24549097 (EID), 28123 (PII)
Keywords: 14-3-3, Aggresomes, Chaperones, Inclusion bodies, Neurodegeneration, Protein aggregation, Protein misfolding
Grant Number: R01 NS050355, NS50355
Publication Note: This NIH-funded author manuscript originally appeared in PubMed Central at
Subject(s): 14-3-3 Proteins/physiology
Neurodegenerative Diseases/physiopathology
Protein Folding
Persistent Link to This Record:
Host Institution: FSU
Is Part Of: Prion.
Issue: iss. 2, vol. 8

Choose the citation style.
Jia, B., Wu, Y., & Zhou, Y. (2014). 14-3-3 and aggresome formation: implications in neurodegenerative diseases. Prion. Retrieved from