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Article

Catalytic domain mutation in CYLD inactivates its enzyme function by structural perturbation and induces cell migration and proliferation.

Biochimica et biophysica acta. General subjects - 1 Sept 2018

Johari Tanu, Maiti Tushar Kanti

Abstract excerpt

Tumor suppressor cylindromatosis protein (CYLD), which specifically cleaves lysine 63-linked ubiquitin chain from its substrate molecules, contributes to myriad of important cellular events including cellular differentiation, oncogenesis, DNA repair and cell cycle control. It is a ubiquitously expressed protein, which negatively regulates NF-kB and JNK signaling pathways and mediates caspase dependent apoptosis...

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Source

Identifiers

PMID: 29807073
DOI: 10.1016/j.bbagen.2018.05.016

Genes

CYLD

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

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Catalytic domain mutation in CYLD inactivates its enzyme function by structural perturbation and induces cell migration and proliferation.PMID 29807073Read ↗

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

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

Identification of the familial cylindromatosis tumour-suppressor gene.Semantic proximity Read ↗

The cylindromatosis gene product, CYLD, interacts with MIB2 to regulate Notch signallingSemantic proximity Read ↗

The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination.Semantic proximity Read ↗

Loss of the tumor suppressor CYLD enhances Wnt/beta-catenin signaling through K63-linked ubiquitination of Dvl.Semantic proximity Read ↗

A Drosophila ortholog of the human cylindromatosis tumor suppressor gene regulates triglyceride content and antibacterial defense.Semantic proximity Read ↗

Update of cylindromatosis gene (CYLD) mutations in Brooke-Spiegler syndrome: novel insights into the role of deubiquitination in cell signaling.Semantic proximity Read ↗

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