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

Keratin 8 phosphorylation by p38 kinase regulates cellular keratin filament reorganization: modulation by a keratin 1-like disease causing mutation.

The Journal of biological chemistry - 29 Mar 2002

Ku Nam-On, Azhar Salman, Omary M Bishr

Abstract excerpt

Keratin 8 (K8) serine 73 occurs within a relatively conserved type II keratin motif ((68)NQSLLSPL) and becomes phosphorylated in cultured cells and organs during mitosis, cell stress, and apoptosis. Here we show that Ser-73 is exclusively phosphorylated in vitro by p38 mitogen-activated protein kinase. In cells, Ser-73 phosphorylation occurs in association with p38 kinase activation and is inhibited by SB203580...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to Cell Line

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Keratins

Share to Mitogen-Activated Protein Kinases

Share to p38 Mitogen-Activated Protein Kinases

Share to Peptide Mapping

Share to Phosphorylation

Share to Transfection

Source

Identifiers

PMID: 11788583
DOI: 10.1074/jbc.M107623200

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Keratin 8 phosphorylation by p38 kinase regulates cellular keratin filament reorganization: modulation by a keratin 1-like disease causing mutation.PMID 11788583Read ↗

A disease- and phosphorylation-related nonmechanical function for keratin 8.Semantic proximity Read ↗

Type II Keratins Are Phosphorylated on a Unique Motif during Stress and Mitosis in Tissues and Cultured CellsSemantic proximity Read ↗

Stress, Apoptosis, and Mitosis Induce Phosphorylation of Human Keratin 8 at Ser-73 in Tissues and Cultured CellsSemantic proximity Read ↗

Generation of a tissue-specific transgenic model for K8 phosphomutants: A tool to investigate the role of K8 phosphorylation during skin carcinogenesis in vivo.Semantic proximity Read ↗

Quantitative phosphoproteomic analysis reveals system-wide signaling pathways regulated by site-specific phosphorylation of Keratin-8 in skin squamous cell carcinoma derived cell line.Semantic proximity Read ↗

Identification of the major physiologic phosphorylation site of human keratin 18: potential kinases and a role in filament reorganization.Semantic proximity Read ↗

Keratin 8 phosphorylation regulates its transamidation and hepatocyte Mallory‐Denk body formationSemantic proximity Read ↗

Keratins in health and disease.Semantic proximity Read ↗

Raf-1 activation disrupts its binding to keratins during cell stress.Semantic proximity Read ↗

Phosphorylation of human keratin 18 serine 33 regulates binding to 14-3-3 proteins.Semantic proximity Read ↗

Posttranslational modifications of keratins and their associated proteins as therapeutic targets in keratin diseases.Semantic proximity Read ↗

Keratin hypersumoylation alters filament dynamics and is a marker for human liver disease and keratin mutation.Semantic proximity Read ↗

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