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

JNK promotes Bax translocation to mitochondria through phosphorylation of 14-3-3 proteins.

The EMBO journal - 21 Apr 2004

Tsuruta Fuminori, Sunayama Jun, Mori Yasunori, Hattori Seisuke, Shimizu Shigeomi, Tsujimoto Yoshihide, Yoshioka Katsuji, Masuyama Norihisa, Gotoh Yukiko

Abstract excerpt

Targeted gene disruption studies have established that the c-Jun NH2-terminal kinase (JNK) is required for the stress-induced release of mitochondrial cytochrome c and apoptosis, and that the Bax subfamily of Bcl-2-related proteins is essential for JNK-dependent apoptosis. However, the mechanism by which JNK regulates Bax has remained unsolved. Here we demonstrate that activated JNK promotes Bax translocation to...

Read the complete abstract on PubMed

Topics

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

Share to 14-3-3 Proteins
Share to bcl-2-Associated X Protein

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Bcl-2-Like Protein 11

Share to Cytochromes c

Share to JNK Mitogen-Activated Protein Kinases

Share to Phosphoserine

Share to Proto-Oncogene Proteins c-bcl-2

Share to Proto-Oncogene Proteins c-jun

Source

Open in PubMed Open full text

Identifiers

PMID: 15071501
DOI: 10.1038/sj.emboj.7600194
PMCID: PMC394248

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

JNK promotes Bax translocation to mitochondria through phosphorylation of 14-3-3 proteins.PMID 15071501Read ↗

The N-terminal conformation of Bax regulates cell commitment to apoptosis.Semantic proximity Read ↗

JNK suppresses apoptosis via phosphorylation of the proapoptotic Bcl-2 family protein BAD.Semantic proximity Read ↗

Cytochrome c release and apoptosis induced by mitochondrial targeting of nuclear orphan receptor TR3.Semantic proximity Read ↗

Direct activation of Bax by p53 mediates mitochondrial membrane permeabilization and apoptosis.Semantic proximity Read ↗

Involvement of the N-terminus of Bax in its intracellular localization and function.Semantic proximity Read ↗

Mitochondrial potassium channel Kv1.3 mediates Bax-induced apoptosis in lymphocytes.Semantic proximity Read ↗

Bax-induced cytochrome c release from mitochondria depends on alpha-helices-5 and -6.Semantic proximity Read ↗

Novel role for JNK as a stress-activated Bcl2 kinase.Semantic proximity Read ↗

Conformation of the Bax C-terminus regulates subcellular location and cell death.Semantic proximity Read ↗

Phosphorylation switches Bax from promoting to inhibiting apoptosis thereby increasing drug resistance.Semantic proximity Read ↗

Ceramide induces p38 MAPK-dependent apoptosis and Bax translocation via inhibition of Akt in HL-60 cells.Semantic proximity Read ↗

Targeting BAX ubiquitin-binding sites reveals that BAX activation is essential for its ubiquitin-dependent degradation.Semantic proximity Read ↗

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