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

Phosphorylation of FADD at serine 194 by CKIalpha regulates its nonapoptotic activities.

Molecular cell - 5 Aug 2005

Alappat Elizabeth C, Feig Christine, Boyerinas Benjamin, Volkland Jörg, Samuels Martin, Murmann Andrea E, Thorburn Andrew, Kidd Vincent J, Slaughter Clive A, Osborn Stephanie L, Winoto Astar, Tang Wei-Jen, Peter Marcus E

Abstract excerpt

FADD is essential for death receptor (DR)-induced apoptosis. However, it is also critical for cell cycle progression and proliferation, activities that are regulated by phosphorylation of its C-terminal Ser194, which has also been implicated in sensitizing cancer cells to chemotherapeutic drugs and in regulating FADD's intracellular localization. We now demonstrate that casein kinase Ialpha (CKIalpha)...

Read the complete abstract on PubMed

Topics

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

Share to Concanavalin A
Share to Cytosol

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fas-Associated Death Domain Protein

Share to Isoquinolines

Share to Jurkat Cells

Share to Paclitaxel

Share to Spindle Apparatus

Share to Tetradecanoylphorbol Acetate

Source

Identifiers

PMID: 16061179
DOI: 10.1016/j.molcel.2005.06.024

Genes

FADD

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 · 11 closest

Phosphorylation of FADD at serine 194 by CKIalpha regulates its nonapoptotic activities.PMID 16061179Read ↗

FADD-calmodulin interaction: a novel player in cell cycle regulation.Semantic proximity Read ↗

Constitutive phosphorylation mutation in Fas-associated death domain (FADD) results in early cell cycle defects.Semantic proximity Read ↗

Phosphorylation of FADD by the kinase CK1α promotes KRASG12D-induced lung cancer.Semantic proximity Read ↗

Regulation of p34cdc2 protein kinase activity by phosphorylation and cyclin binding.Semantic proximity Read ↗

Attenuation of DNA damage checkpoint by PBK, a novel mitotic kinase, involves protein-protein interaction with tumor suppressor p53.Semantic proximity Read ↗

Cooperative phosphorylation of FADD by Aur-A and Plk1 in response to taxol triggers both apoptotic and necrotic cell death.Semantic proximity Read ↗

A novel role for Cdk1/cyclin B in regulating B-raf activation at mitosis.Semantic proximity Read ↗

Cell cycle-dependent expression of cIAP2 at G2/M phase contributes to survival during mitotic cell cycle arrest.Semantic proximity Read ↗

The adapter protein FADD provides an alternate pathway for entry into the cell cycle by regulating APC/C-Cdh1 E3 ubiquitin ligase activity.Semantic proximity Read ↗

Degradation of cyclin A is regulated by acetylation.Semantic proximity Read ↗

Cells lacking IKKα show nuclear cyclin D1 overexpression and a neoplastic phenotype: role of IKKα as a tumor suppressor.Semantic proximity Read ↗

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