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TRIM28 functions as a negative regulator of aggresome formation

Authors
Chang, JeeyoonHwang, Hyun JungKim, ByungjuChoi, Yeon-GilPark, JooriPark, YeonkyoungLee, Ban SeokPark, HeedoYoon, Min JiWoo, Jae-SungKim, ChunghoPark, Man-SeongLee, Jong-BongKim, Yoon Ki
Issue Date
2-12월-2021
Publisher
TAYLOR & FRANCIS INC
Keywords
Aggrephagy; CTIF; DCTN1; influenza A virus; EIF2AK2
Citation
AUTOPHAGY, v.17, no.12, pp.4231 - 4248
Indexed
SCIE
SCOPUS
Journal Title
AUTOPHAGY
Volume
17
Number
12
Start Page
4231
End Page
4248
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/130216
DOI
10.1080/15548627.2021.1909835
ISSN
1554-8627
Abstract
Selective recognition and elimination of misfolded polypeptides are crucial for protein homeostasis. When the ubiquitin-proteasome system is impaired, misfolded polypeptides tend to form small cytosolic aggregates and are transported to the aggresome and eventually eliminated by the autophagy pathway. Despite the importance of this process, the regulation of aggresome formation remains poorly understood. Here, we identify TRIM28/TIF1 beta/KAP1 (tripartite motif containing 28) as a negative regulator of aggresome formation. Direct interaction between TRIM28 and CTIF (cap binding complex dependent translation initiation factor) leads to inefficient aggresomal targeting of misfolded polypeptides. We also find that either treatment of cells with poly I:C or infection of the cells by influenza A viruses triggers the phosphorylation of TRIM28 at S473 in a way that depends on double-stranded RNA-activated protein kinase. The phosphorylation promotes association of TRIM28 with CTIF, inhibits aggresome formation, and consequently suppresses viral proliferation. Collectively, our data provide compelling evidence that TRIM28 is a negative regulator of aggresome formation.
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