2015
DOI: 10.1111/febs.13540
|View full text |Cite
|
Sign up to set email alerts
|

p62/SQSTM1 functions as a signaling hub and an autophagy adaptor

Abstract: and ichimura-ys@med.niigata-u.ac.jp p62/SQSTM1 is a stress-inducible cellular protein that is conserved among metazoans 20 but not in plants and fungi. p62/SQSTM1 has multiple domains that mediate its interactions with various binding partners, and it serves as a signaling hub for diverse cellular events such as amino-acid sensing and the oxidative stress response. In addition, p62/SQSTM1 functions as a selective autophagy receptor for degradation of ubiqutinated substrates. Herein we delineate the current kno… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1

Citation Types

14
558
1
4

Year Published

2016
2016
2024
2024

Publication Types

Select...
7
1

Relationship

0
8

Authors

Journals

citations
Cited by 681 publications
(577 citation statements)
references
References 46 publications
14
558
1
4
Order By: Relevance
“…Abnormally folded proteins can aggregate and form inclusion bodies in the cell, thereby perturbing intracellular signaling and cell activity. Although these aggregates can be eliminated by p62-mediated ALS (25,26), the accumulation of p62-containing aggregates indicates an impairment of the ALS in embryonic cells of diabetic mice. Three proteins associated with neurodegenerative diseases, α-Syn, Parkin, and Htt, also form aggregates in the embryos of diabetic mice.…”
Section: Discussionmentioning
confidence: 99%
See 2 more Smart Citations
“…Abnormally folded proteins can aggregate and form inclusion bodies in the cell, thereby perturbing intracellular signaling and cell activity. Although these aggregates can be eliminated by p62-mediated ALS (25,26), the accumulation of p62-containing aggregates indicates an impairment of the ALS in embryonic cells of diabetic mice. Three proteins associated with neurodegenerative diseases, α-Syn, Parkin, and Htt, also form aggregates in the embryos of diabetic mice.…”
Section: Discussionmentioning
confidence: 99%
“…Aggregates of ubiquitinylated proteins are subject to ALS clearance, mediated by ubiquitin-binding protein p62 (25,26). Doublelabeling with Proteostat to detect protein aggregates and an antibody to detect p62 revealed colocalization of protein aggregates and p62 ( Fig.…”
Section: Significancementioning
confidence: 94%
See 1 more Smart Citation
“…17,[20][21][22] The SQSTM1 (sequestosome 1, p62) protein is a ubiquitin-binding scaffold molecule that plays a key role in autophagic degradation of ubiquitinated proteins, [23][24][25][26][27][28][29] and the degradation of SQSTM1 with tumor-related antigen may promote T-cell-mediated immunity. [30][31][32] Colorectal cancer represents a heterogeneous group of neoplasms resulting from genomic and epigenomic alterations, which influence and are influenced by tumor-host interactions.…”
Section: Introductionmentioning
confidence: 99%
“…Therefore, elucidating the molecular mechanisms underlying pancreatic β-cell dysfunction is a key to understanding the pathology of diabetes [3,4]. Sequestosome 1 (SQSTM1, referred to hereafter as p62) is a multifunctional scaffold protein that can interact with several signaling pathways through its functional subdomains, including the Phox and Bem1 (PB1) domain, zinc-finger domain, TNF receptor-associated factor 6 (TRAF6)-binding domain, and Kelch-like ECHassociated protein 1 (Keap1) interacting region (KIR) [5][6][7]. p62/SQSTM1 can activate the antioxidant response by interacting with the Keap1-Nrf2 pathway [8][9][10].…”
mentioning
confidence: 99%