Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

FAT10, a ubiquitin-independent signal for proteasomal degradation.

Molecular and cellular biology - 1 May 2005

Hipp Mark Steffen, Kalveram Birte, Raasi Shahri, Groettrup Marcus, Schmidtke Gunter

Abstract excerpt

FAT10 is a small ubiquitin-like modifier that is encoded in the major histocompatibility complex and is synergistically inducible by tumor necrosis factor alpha and gamma interferon. It is composed of two ubiquitin-like domains and possesses a free C-terminal diglycine motif that is required for the formation of FAT10 conjugates. Here we show that unconjugated FAT10 and a FAT10 conjugate were rapidly degraded by...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adaptor Proteins, Signal Transducing
Share to Green Fluorescent Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Half-Life

Share to Proteasome Endopeptidase Complex

Share to Recombinant Fusion Proteins

Share to Transfection

Share to Ubiquitin

Share to Ubiquitins

Source

Open in PubMed Open full text

Identifiers

PMID: 15831455
DOI: 10.1128/MCB.25.9.3483-3491.2005
PMCID: PMC1084302

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

FAT10, a ubiquitin-independent signal for proteasomal degradation.PMID 15831455Read ↗

FAT10/diubiquitin-like protein-deficient mice exhibit minimal phenotypic differences.Semantic proximity Read ↗

Investigations into the auto-FAT10ylation of the bispecific E2 conjugating enzyme UBA6-specific E2 enzyme 1.Semantic proximity Read ↗

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

Characterization of NFkappaB activation by detection of green fluorescent protein-tagged IkappaB degradation in living cells.Semantic proximity Read ↗

The ubiquitin-activating enzyme is required for lysosomal degradation of cellular proteins under stress.Semantic proximity Read ↗

Shared pathways of IkappaB kinase-induced SCF(betaTrCP)-mediated ubiquitination and degradation for the NF-kappaB precursor p105 and IkappaBalpha.Semantic proximity Read ↗

Efficient internalization of MHC I requires lysine-11 and lysine-63 mixed linkage polyubiquitin chains.Semantic proximity Read ↗

Ubiquitin-mediated proteolysis of a short-lived regulatory protein depends on its cellular localization.Semantic proximity Read ↗

Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation and subsequent degradation of IkappaBalpha.Semantic proximity Read ↗

Ubiquitinylation Is Not an Absolute Requirement for Degradation of c-Jun Protein by the 26 S ProteasomeSemantic proximity Read ↗

c-Fos proto-oncoprotein is degraded by the proteasome independently of its own ubiquitinylation in vivo.Semantic proximity Read ↗

Negative feedback loop in T cell activation through IkappaB kinase-induced phosphorylation and degradation of Bcl10.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.