FAT10ylation as a signal for proteasomal degradation.

No abstract is available for this paper.

• Publication year

  2014

• Venue

  Biochimica et Biophysica Acta

• Publication date

  Unknown publication date

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1016/j.bbamcr.2013.01.009PMID 23333871
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• FAT10 is a proteasomal degradation signal that is itself regulated by ubiquitination

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• FAT10 and NUB1L bind to the VWA domain of Rpn10 and Rpn1 to enable proteasome-mediated proteolysis

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• Mechanistic Studies on Activation of Ubiquitin and Di-ubiquitin-like Protein, FAT10, by Ubiquitin-like Modifier Activating Enzyme 6, Uba6*

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• Modification of the inflammatory mediator LRRFIP2 by the ubiquitin-like protein FAT10 inhibits its activity during cellular response to LPS.

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• The FAT10- and ubiquitin-dependent degradation machineries exhibit common and distinct requirements for MHC class I antigen presentation

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• The proteomic analysis of endogenous FAT10 substrates identifies p62/SQSTM1 as a substrate of FAT10ylation

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• FAT10 mediates the effect of TNF-α in inducing chromosomal instability

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• USE1 is a bispecific conjugating enzyme for ubiquitin and FAT10, which FAT10ylates itself in cis.

  2010cited by this paper
• USE 1 is a bispecifi c conjugating enzyme for ubiquitin and FAT 10 , which FAT 10 ylates itself in cis

  2010cited by this paper
• DUBs at a glance

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• Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation.

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• Maturation of human dendritic cells is accompanied by functional remodelling of the ubiquitin-proteasome system.

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• Degradation of FAT10 by the 26S proteasome is independent of ubiquitylation but relies on NUB1L

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• Fat10 is an epigenetic marker for liver preneoplasia in a drug-primed mouse model of tumorigenesis.

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• Arsenic trioxide stimulates SUMO‐2/3 modification leading to RNF4‐dependent proteolytic targeting of PML

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• Arsenic degrades PML or PML–RARα through a SUMO-triggered RNF4/ubiquitin-mediated pathway

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• Proinflammatory cytokines cause FAT10 upregulation in cancers of liver and colon

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• Proteasome subunit Rpn13 is a novel ubiquitin receptor

  2008cited by this paper
• Activating the ubiquitin family: UBA6 challenges the field.

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• The ubiquitin-like modifier FAT10 interacts with HDAC6 and localizes to aggresomes under proteasome inhibition

  2008cited by this paper
• Identification of seven new humanMHC class I region genes around theHLA-F locus

  2007cited by this paper
• E1-L2 activates both ubiquitin and FAT10.

  2007cited by this paper
• UBE 1 L 2 , a Novel E 1 Enzyme Specific for Ubiquitin *

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• Cloning and characterization of a gene encoding the human putative ubiquitin conjugating enzyme E2Z (UBE2Z)

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• UBE1L2, a Novel E1 Enzyme Specific for Ubiquitin*♦

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• Dual E1 activation systems for ubiquitin differentially regulate E2 enzyme charging

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• Modification of proteins by ubiquitin and ubiquitin-like proteins.

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• Role of ubiquitin-like protein FAT10 in epithelial apoptosis in renal disease.

  2006cited by this paper
• FAT10 Plays a Role in the Regulation of Chromosomal Stability*

  2006cited by this paper
• FAT10/Diubiquitin-Like Protein-Deficient Mice Exhibit Minimal Phenotypic Differences

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• The UBA Domains of NUB1L Are Required for Binding but Not for Accelerated Degradation of the Ubiquitin-like Modifier FAT10*

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• Crystal Structure of the Interferon-induced Ubiquitin-like Protein ISG15*[boxs]

  2005cited by this paper
• FAT10, a Ubiquitin-Independent Signal for Proteasomal Degradation

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• Interaction of NUB1 with the proteasome subunit S5a.

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• NEDD8 Ultimate Buster-1L Interacts with the Ubiquitin-like Protein FAT10 and Accelerates Its Degradation*

  2004cited by this paper
• Expression of the FAT10 gene is highly upregulated in hepatocellular carcinoma and other gastrointestinal and gynecological cancers

  2003cited by this paper
• The Ubiquitin-like Protein FAT10 Forms Covalent Conjugates and Induces Apoptosis*

  2001cited by this paper
• Targeting of NEDD8 and Its Conjugates for Proteasomal Degradation by NUB1*

  2001cited by this paper
• NUB1, a NEDD8-interacting Protein, Is Induced by Interferon and Down-regulates the NEDD8 Expression*

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• The ubiquitin system

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• Basic Medical Research Award. The ubiquitin system.

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• A MHC-encoded ubiquitin-like protein (FAT10) binds noncovalently to the spindle assembly checkpoint protein MAD2.

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• Activation of the heat-stable polypeptide of the ATP-dependent proteolytic system.

  1981influential reference
• A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes.

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• Co-sedimentation is the key to the structural investigation of wild-type FAT10

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• Beyond degradation tags: How FAT10 and ubiquitin shape substrate energy landscapes

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• FAT10 inhibits TRIM21 to down-regulate antiviral type-I interferon secretion

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• FAT10 mediates the sorafenib-resistance of hepatocellular carcinoma cells by stabilizing E3 ligase NEDD4 to enhance PTEN/AKT pathway-induced autophagy.

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• The Thermodynamic Properties of Fat10ylated Proteins Are Regulated by the Fat10ylation Site

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• Phosphorylated FAT10 Is More Efficiently Conjugated to Substrates, Does Not Bind to NUB1L, and Does Not Alter Degradation by the Proteasome

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