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Article

Deubiquitinating activity of CYLD is impaired by SUMOylation in neuroblastoma cells.

Oncogene - 23 Apr 2015

Kobayashi T, Masoumi K C, Massoumi R

Abstract excerpt

CYLD is a deubiquitinating (DUB) enzyme that has a pivotal role in modulating nuclear factor kappa B (NF-κB) signaling pathways by removing the lysine 63- and linear-linked ubiquitin chain from substrates such as tumor necrosis factor receptor-associated factor 2 (TRAF2) and TRAF6. Loss of CYLD activity is associated with tumorigenicity, and levels of CYLD are lost or downregulated in different types of human...

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Source

Identifiers

PMID: 24909169
DOI: 10.1038/onc.2014.159

Genes

CYLD
TRAF2
TRAF6

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

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Deubiquitinating activity of CYLD is impaired by SUMOylation in neuroblastoma cells.PMID 24909169Read ↗

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CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members.Semantic proximity Read ↗

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Impaired regulation of NF-kappaB and increased susceptibility to colitis-associated tumorigenesis in CYLD-deficient mice.Semantic proximity Read ↗

NF-kappaB is essential for induction of CYLD, the negative regulator of NF-kappaB: evidence for a novel inducible autoregulatory feedback pathway.Semantic proximity Read ↗

CYLD negatively regulates cell-cycle progression by inactivating HDAC6 and increasing the levels of acetylated tubulin.Semantic proximity Read ↗

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