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

Direct binding of the Na--H exchanger NHE1 to ERM proteins regulates the cortical cytoskeleton and cell shape independently of H(+) translocation.

Molecular cell - 1 Dec 2000

Denker S P, Huang D C, Orlowski J, Furthmayr H, Barber D L

Abstract excerpt

The association of actin filaments with the plasma membrane maintains cell shape and adhesion. Here, we show that the plasma membrane ion exchanger NHE1 acts as an anchor for actin filaments to control the integrity of the cortical cytoskeleton. This occurs through a previously unrecognized structural link between NHE1 and the actin binding proteins ezrin, radixin, and moesin (ERM). NHE1 and ERM proteins...

Read the complete abstract on PubMed

Topics

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

Share to Blood Proteins
Share to Cell Size
Share to Focal Adhesions

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

Share to Hydrogen

Share to Ion Transport

Share to Protons

Share to Sodium-Hydrogen Exchangers

Share to Stress Fibers

Source

Identifiers

PMID: 11163215
DOI: 10.1016/s1097-2765(00)00139-8

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

Direct binding of the Na--H exchanger NHE1 to ERM proteins regulates the cortical cytoskeleton and cell shape independently of H(+) translocation.PMID 11163215Read ↗

A NHERF binding site links the betaPDGFR to the cytoskeleton and regulates cell spreading and migration.Semantic proximity Read ↗

A glimpse of the ERM proteinsSemantic proximity Read ↗

Inside Out: Targeting NHE1 as an Intracellular and Extracellular Regulator of Cancer ProgressionSemantic proximity Read ↗

Pathophysiological Roles of Actin-Binding Scaffold Protein, EzrinSemantic proximity Read ↗

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

Cellular functions of GEF-H1, a microtubule-regulated Rho-GEF: is altered GEF-H1 activity a crucial determinant of disease pathogenesis?Semantic proximity Read ↗

NHERF1/EBP50 controls lactation by establishing basal membrane polarity complexes with prolactin receptor.Semantic proximity Read ↗

The cellular distribution of Na+/H+ exchanger regulatory factor 1 is determined by the PDZ-I domain and regulates the malignant progression of breast cancer.Semantic proximity Read ↗

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

Ezrin Phosphorylation at T567 Modulates Cell Migration, Mechanical Properties, and Cytoskeletal Organization.Semantic proximity Read ↗

RACK1 associates with NHE5 in focal adhesions and positively regulates the transporter activity.Semantic proximity Read ↗

Ezrin is concentrated in the apical microvilli of a wide variety of epithelial cells whereas moesin is found primarily in endothelial cellsSemantic proximity Read ↗

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