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

Rho-Kinase Phosphorylates COOH-terminal Threonines of Ezrin/Radixin/Moesin (ERM) Proteins and Regulates Their Head-to-Tail Association

9 Feb 1998

Abstract excerpt

The ezrin/radixin/moesin (ERM) proteins are involved in actin filament/plasma membrane interaction that is regulated by Rho. We examined whether ERM proteins are directly phosphorylated by Rho-associated kinase (Rho-kinase), a direct target of Rho. Recombinant full-length and COOH-terminal half radixin were incubated with constitutively active catalytic domain of Rho-kinase, and approximately 30 and approximately...

Read the complete abstract on PubMed

Topics

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

Share to Cell Adhesion Molecules Research
Share to Neurofibromatosis and Schwannoma Cases
Share to Signaling Pathways in Disease

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 9456324
DOI: 10.1083/jcb.140.3.647

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Rho-Kinase Phosphorylates COOH-terminal Threonines of Ezrin/Radixin/Moesin (ERM) Proteins and Regulates Their Head-to-Tail AssociationPMID 9456324Read ↗

A glimpse of the ERM proteinsSemantic proximity Read ↗

Identification and relevance of the CD95-binding domain in the N-terminal region of ezrin.Semantic proximity Read ↗

ERM proteins in cancer progressionSemantic proximity Read ↗

ERM (ezrin/radixin/moesin) family: from cytoskeleton to signal transductionSemantic proximity Read ↗

A gene family consisting of ezrin, radixin and moesin Its specific localization at actin filament/plasma membrane association sitesSemantic proximity Read ↗

Protein phosphatase 1α mediates ceramide-induced ERM protein dephosphorylation: a novel mechanism independent of phosphatidylinositol 4, 5-biphosphate (PIP2) and myosin/ERM phosphatase.Semantic proximity Read ↗

Identification of EBP50: A PDZ-containing Phosphoprotein that Associates with Members of the Ezrin-Radixin-Moesin FamilySemantic proximity Read ↗

Epidermal growth factor-induced cellular invasion requires sphingosine-1-phosphate/sphingosine-1-phosphate 2 receptor-mediated ezrin activation.Semantic proximity Read ↗

Structural basis of adhesion-molecule recognition by ERM proteins revealed by the crystal structure of the radixin-ICAM-2 complex.Semantic proximity Read ↗

Radixin is a novel member of the band 4.1 family.Semantic proximity Read ↗

Normal development of mice and unimpaired cell adhesion/cell motility/actin-based cytoskeleton without compensatory up-regulation of ezrin or radixin in moesin gene knockout.Semantic proximity Read ↗

Moesin functions antagonistically to the Rho pathway to maintain epithelial integrity.Semantic proximity Read ↗

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