ArticleCell research2017
Ubiquitylation of p62/sequestosome1 activates its autophagy receptor function and controls selective autophagy upon ubiquitin stress.
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Article in Cell research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 117 papers, 1 of them a synthesis that pooled it.
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117citing papers in PubMed, 1 pooled it
12.6field-weighted citation impact, top 1% of its field
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Who cites it
117 citing papers in PubMed, 1 synthesis or guideline pooled it, 183 citations in OpenAlex.
- Non-coding RNAs' pivotal importance in modulation of cancer sensitivity to Topotecan: a systematic review.Medical oncology (Northwood, London, England) · 2025Pooled it
- Autophagy and ubiquitination in important swine viral infections: Host defense and viral antagonism.Virulence · 2026Review
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- A quantitative redox proteome of the human muscle response to exercise.bioRxiv : the preprint server for biology · 2026Article
- UBE2N deficiency contributes to MASH development via p62-regulated mitophagy and PANoptosis.Nature metabolism · 2026Article
- The role of E3 ubiquitin ligases in selective types of macroautophagy.EMBO reports · 2026Review
- Ubiquitin Ligases in pro-atrophic and antiatrophic signaling cascades in muscles.Molecular biology reports · 2026Review
- Lysine lactylation-mediated post-translational modification: Molecular mechanisms and therapeutic target exploration in tumour drug resistance.Clinical and translational medicine · 2026Review
- Ubiquitin-specific protease 48 drives malignant progression of colorectal cancer by suppressing autophagy through stabilizing sequestosome 1.Cell death and differentiation · 2026Article
- LAMTOR5 promotes hepatoma growth in mice by disrupting LC3-p62-mediated autophagy and preventing p62 proteasome degradation.Acta pharmacologica Sinica · 2026Article
- Resveratrol Attenuates Liver Inflammation in Non-Alcoholic Fatty Liver Disease by Activating PINK1-Mediated Mitophagy.Animals : an open access journal from MDPI · 2026Article
- Post-translational modifications of selective autophagy receptors: orchestrating cellular homeostasis, disease pathogenesis, and therapeutic opportunities.Cellular & molecular biology letters · 2026Review
- Ro 31-8220 suppresses bladder cancer progression via enhancing autophagy in vitro and in vivo.FEBS open bio · 2025Article
- Genetic and proteomic analysis identifies BAG3 as an amyloid-responsive regulator of neuronal proteostasis.Acta neuropathologica · 2025Article
- API5 Phosphorylation Promotes Antiviral Immunity by Inhibiting Degradation of Cytosolic RNA Sensor RLRs.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- TBK1 is a signaling hub in coordinating stress-adaptive mechanisms in head and neck cancer progression.Autophagy · 2025Article
- Targeting Lipophagy in Liver Diseases: Impact on Oxidative Stress and Steatohepatitis.Antioxidants (Basel, Switzerland) · 2025Review
- TRIM25 ubiquitinates and degrades p62/SQSTM1 to suppress autophagy.Acta biochimica et biophysica Sinica · 2025Article
- CXCL13 Damages Blood Spinal Cord Barrier by Promoting RNF6/Sqstm1-Ubiquitination Induced Autophagy in Experimental Allergic Encephalomyelitis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Identification of new candidates regulating autophagy-dependent midgut degradation in Drosophila melanogaster.Cell death discovery · 2025Article
57 more citing papers are in PubMed but not listed here.
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Authors and funding
25 authors at 10 institutions in 4 countries.
Hong PengKey Laboratory of Systems Biology, CAS Center for Excellence in Molecular Cell Science, Innovation Center for Cell Signaling Network, Shanghai 200031, China.
Jiao YangKey Laboratory of Systems Biology, CAS Center for Excellence in Molecular Cell Science, Innovation Center for Cell Signaling Network, Shanghai 200031, China.
Guangyi LiKey Laboratory of Systems Biology, CAS Center for Excellence in Molecular Cell Science, Innovation Center for Cell Signaling Network, Shanghai 200031, China.
Qing YouKey Laboratory of Systems Biology, CAS Center for Excellence in Molecular Cell Science, Innovation Center for Cell Signaling Network, Shanghai 200031, China.
Wen HanKey Laboratory of Systems Biology, CAS Center for Excellence in Molecular Cell Science, Innovation Center for Cell Signaling Network, Shanghai 200031, China.
Tianrang LiKey Laboratory of Systems Biology, CAS Center for Excellence in Molecular Cell Science, Innovation Center for Cell Signaling Network, Shanghai 200031, China.
Daming GaoKey Laboratory of Systems Biology, CAS Center for Excellence in Molecular Cell Science, Innovation Center for Cell Signaling Network, Shanghai 200031, China.
Xiaoduo XieKey Laboratory of Systems Biology, CAS Center for Excellence in Molecular Cell Science, Innovation Center for Cell Signaling Network, Shanghai 200031, China.
Byung-Hoon LeeDepartment of Cell Biology, Harvard Medical School, 240 Longwood Ave, Boston, MA 02115, USA.
Juan DuDepartment of Hematology, Changzheng Hospital, The Second Military Medical University, 415 Fengyang Road, Shanghai 200003, China.
Jian HouDepartment of Hematology, Changzheng Hospital, The Second Military Medical University, 415 Fengyang Road, Shanghai 200003, China.
Tao ZhangDepartment of Laboratory Medicine, Huashan Hospital, Fudan University, 12 Central Urumqi Road, Shanghai 200040, China.
Hai RaoDepartment of Molecular Medicine, University of Texas Health Science Center at San Antonio, San Antonio, Texas 78229, USA.
Ying HuangInstitute of Biochemistry and Cell Biology, Chinese Academy of Sciences, 320 Yueyang Road, Shanghai 200031, China.
Qinrun LiKey Laboratory of Systems Biology, CAS Center for Excellence in Molecular Cell Science, Innovation Center for Cell Signaling Network, Shanghai 200031, China.
Rong ZengKey Laboratory of Systems Biology, CAS Center for Excellence in Molecular Cell Science, Innovation Center for Cell Signaling Network, Shanghai 200031, China.
Lijian HuiInstitute of Biochemistry and Cell Biology, Chinese Academy of Sciences, 320 Yueyang Road, Shanghai 200031, China.
Hongyan WangKey Laboratory of Systems Biology, CAS Center for Excellence in Molecular Cell Science, Innovation Center for Cell Signaling Network, Shanghai 200031, China.
Qin XiaState Key Laboratory of Proteomics, National Center of Biomedical Analysis, Institute of Basic Medical Sciences, Beijing 100850, China.
Xuemin ZhangState Key Laboratory of Proteomics, National Center of Biomedical Analysis, Institute of Basic Medical Sciences, Beijing 100850, China.
Yongning HeInstitute of Biochemistry and Cell Biology, Chinese Academy of Sciences, 320 Yueyang Road, Shanghai 200031, China.
Masaaki KomatsuDepartment of Biochemistry, School of Medicine Niigata University, 757, Ichibancho, Asahimachidori, Chuo-ku, Niigata 951-8510, Japan.
Ivan DikicMolecular Signaling, Institute of Biochemistry II, Goethe University School of Medicine, 60590 Frankfurt am Main, Germany.
Daniel FinleyDepartment of Cell Biology, Harvard Medical School, 240 Longwood Ave, Boston, MA 02115, USA.
Ronggui HuKey Laboratory of Systems Biology, CAS Center for Excellence in Molecular Cell Science, Innovation Center for Cell Signaling Network, Shanghai 200031, China.
Center for Excellence in Molecular Cell Science · CNChinese Academy of Sciences · CNHarvard University · USNational Center of Biomedical Analysis · CNSecond Military Medical University · CNUniversity of Chinese Academy of Sciences · CNGoethe University Frankfurt · DEHuashan Hospital · CNNiigata University · JPThe University of Texas Health Science Center at San Antonio · US
Funding
UBIQUITIN-PROTEIN CONJUGATES AND FUSIONSR01GM043601 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI FINLEY, DANIEL J · 1990 to 2020
$4.3MUbiquitin chain editing by the mammalian proteasomeR01GM095526 · NIGMS · HARVARD MEDICAL SCHOOL · PI FINLEY, DANIEL J · 2011 to 2014
$1.8MNIGMS NIH HHS R01 GM043601NIGMS NIH HHS R01 GM095526
Abstract
Alterations in cellular ubiquitin (Ub) homeostasis, known as Ub stress, feature and affect cellular responses in multiple conditions, yet the underlying mechanisms are incompletely understood. Here we report that autophagy receptor p62/sequestosome-1 interacts with E2 Ub conjugating enzymes, UBE2D2 and UBE2D3. Endogenous p62 undergoes E2-dependent ubiquitylation during upregulation of Ub homeostasis, a condition termed as Ub
Indexed as
AutophagyUbiquitinationAnimalsFibroblastsHeat-Shock ResponseHEK293 CellsHeLa CellsHumansMicePhosphorylationPhosphoserinePolyubiquitinProteasome InhibitorsProtein BindingProtein DomainsProtein MultimerizationPhosphoserinePolyubiquitinProteasome InhibitorsSequestosome-1 ProteinSQSTM1 protein, humanSqstm1 protein, mouseUBE2D2 protein, humanUBE2D3 protein, humanUbiquitinUbiquitin-Conjugating Enzymes
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.