p62/SQSTM1 functions as a signaling hub and an autophagy adaptor (Q28081418)

Yoshinobu Ichimura

series ordinal

2

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language of work or name

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December 2015

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282

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PubMed

issue

24

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PubMed

page(s)

4672-8

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P62/SQSTM1 at the interface of aging, autophagy, and disease

PubMed

cites work

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Interaction domains of p62: a bridge between p62 and selective autophagy

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The role of the selective adaptor p62 and ubiquitin-like proteins in autophagy.

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TCR signaling to NF-κB and mTORC1: Expanding roles of the CARMA1 complex

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Feedback on Fat: p62-mTORC1-Autophagy Connections

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Interactions between autophagy receptors and ubiquitin-like proteins form the molecular basis for selective autophagy.

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Oxidative stress and autophagy: the clash between damage and metabolic needs

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Physiological significance of selective degradation of p62 by autophagy

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Fighting disease by selective autophagy of aggregate-prone proteins

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Selective autophagy mediated by autophagic adapter proteins

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Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids

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Regulation of mTORC1 by amino acids

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p62 is a key regulator of nutrient sensing in the mTORC1 pathway.

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K63 polyubiquitination and activation of mTOR by the p62-TRAF6 complex in nutrient-activated cells

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Molecular mechanisms of the Keap1–Nrf2 pathway in stress response and cancer evolution

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The emerging role of the Nrf2-Keap1 signaling pathway in cancer

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Structural basis for defects of Keap1 activity provoked by its point mutations in lung cancer

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Kinetic, Thermodynamic, and Structural Characterizations of the Association between Nrf2-DLGex Degron and Keap1

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A noncanonical mechanism of Nrf2 activation by autophagy deficiency: direct interaction between Keap1 and p62.

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Phosphorylation of p62 activates the Keap1-Nrf2 pathway during selective autophagy

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p62/SQSTM1 is a target gene for transcription factor NRF2 and creates a positive feedback loop by inducing antioxidant response element-driven gene transcription

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Keap1 degradation by autophagy for the maintenance of redox homeostasis

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p62/Sequestosome-1, Autophagy-related Gene 8, and Autophagy in Drosophila Are Regulated by Nuclear Factor Erythroid 2-related Factor 2 (NRF2), Independent of Transcription Factor TFEB.

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Crystal structure of the ubiquitin-associated (UBA) domain of p62 and its interaction with ubiquitin.

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Proteotoxic stress induces phosphorylation of p62/SQSTM1 by ULK1 to regulate selective autophagic clearance of protein aggregates

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Serine 403 Phosphorylation of p62/SQSTM1 Regulates Selective Autophagic Clearance of Ubiquitinated Proteins

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TBK-1 Promotes Autophagy-Mediated Antimicrobial Defense by Controlling Autophagosome Maturation

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Sestrin2 promotes Unc-51-like kinase 1 mediated phosphorylation of p62/sequestosome-1

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The Atg8 family: multifunctional ubiquitin-like key regulators of autophagy

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p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy

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Structural basis for sorting mechanism of p62 in selective autophagy

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p62 Targeting to the autophagosome formation site requires self-oligomerization but not LC3 binding

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The selective autophagy receptor p62 forms a flexible filamentous helical scaffold

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p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both

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Proteasome dysfunction activates autophagy and the Keap1-Nrf2 pathway

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Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice

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Dissection of the role of p62/Sqstm1 in activation of Nrf2 during xenophagy

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Coordination of mitophagy and mitochondrial biogenesis during ageing in C. elegans

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p62 Is a common component of cytoplasmic inclusions in protein aggregation diseases

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SQSTM1 is a pathogenic target of 5q copy number gains in kidney cancer

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SQSTM1 mutations--bridging Paget disease of bone and ALS/FTLD.

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21 January 2018

Identifiers

DOI

10.1111/FEBS.13540

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Consolidated OpenCitations Corpus – April 2017

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Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

26432171

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Consolidated OpenCitations Corpus – April 2017