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Misfolded polypeptides are selectively recognized and transported toward aggresomes by a CED complex

Title
Misfolded polypeptides are selectively recognized and transported toward aggresomes by a CED complex
Author
최준호
Keywords
MESSENGER-RNA DECAY; PROTEIN-QUALITY CONTROL; ELONGATION-FACTOR 1A; CAP-BINDING COMPLEX; CBP80/20-DEPENDENT TRANSLATION; NEURODEGENERATIVE DISEASES; CYTOPLASMIC DYNEIN; AGGREGATION; HISTONE; DEGRADATION
Issue Date
2017-06
Publisher
NATURE PUBLISHING GROUP
Citation
NATURE COMMUNICATIONS, v. 8, Article no. 15730
Abstract
Misfolded polypeptides are rapidly cleared from cells via the ubiquitin-proteasome system (UPS). However, when the UPS is impaired, misfolded polypeptides form small cytoplasmic aggregates, which are sequestered into an aggresome and ultimately degraded by aggrephagy. Despite the relevance of the aggresome to neurodegenerative proteinopathies, the molecular mechanisms underlying aggresome formation remain unclear. Here we show that the CTIF-eEF1A1-DCTN1 (CED) complex functions in the surveillance of either pre-existing or newly synthesized polypeptides by linking two molecular events: selective recognition and aggresomal targeting of misfolded polypeptides. These events are accompanied by CTIF sequestration into the aggresome, preventing the additional synthesis of misfolded polypeptides from mRNAs bound by nuclear cap-binding complex. These events render cells more resistant to apoptosis induced by proteotoxic stresses. Collectively, our data provide compelling evidence for a previously unappreciated protein surveillance pathway and a regulatory gene expression network for coping with misfolded polypeptides.
URI
https://www.nature.com/articles/ncomms15730http://repository.hanyang.ac.kr/handle/20.500.11754/114508
ISSN
2041-1723
DOI
10.1038/ncomms15730
Appears in Collections:
COLLEGE OF NATURAL SCIENCES[S](자연과학대학) > LIFE SCIENCE(생명과학과) > Articles
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