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

Critical role of the isoform-specific region in alpha1-Na,K-ATPase trafficking and protein Kinase C-dependent regulation.

Biochemistry - 4 May 2010

Sottejeau Yoann, Belliard Aude, Duran Marie-Josée, Pressley Thomas A, Pierre Sandrine V

Abstract excerpt

The isoform-specific region (ISR) is a region of structural heterogeneity among the four isoforms of the catalytic alpha-subunit of the Na,K-ATPase and an important structural determinant for isoform-specific functions. In the present study, we examined the role of a potential dileucine clathrin adaptor recognition motif [DE]XXXL[LI] embedded within the alpha1-ISR. To this end, a rat alpha1 construct where...

Read the complete abstract on PubMed

Topics

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

Share to Biotinylation
Share to Enzyme Inhibitors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Kidney

Share to Opossums

Share to Ouabain

Share to Protein Isoforms

Share to Protein Kinase C

Share to Sodium-Potassium-Exchanging ATPase

Source

Open in PubMed Open full text

Identifiers

PMID: 20302352
DOI: 10.1021/bi9021999
PMCID: PMC4303032

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

Critical role of the isoform-specific region in alpha1-Na,K-ATPase trafficking and protein Kinase C-dependent regulation.PMID 20302352Read ↗

Modulation of Na(+)-K(+)-ATPase cell surface abundance through structural determinants on the α1-subunit.Semantic proximity Read ↗

Tyrosine 537 within the Na+,K+-ATPase alpha-subunit is essential for AP-2 binding and clathrin-dependent endocytosis.Semantic proximity Read ↗

Heterogeneity of signal transduction by Na-K-ATPase α-isoforms: role of Src interaction.Semantic proximity Read ↗

Structural basis for alpha1 versus alpha2 isoform-distinct behavior of the Na,K-ATPase.Semantic proximity Read ↗

Clathrin-mediated endocytosis of Na+,K+-ATPase in response to parathyroid hormone requires ERK-dependent phosphorylation of Ser-11 within the alpha1-subunit.Semantic proximity Read ↗

Na+, K+-ATPase isozyme diversity; comparative biochemistry and physiological implications of novel functional interactions.Semantic proximity Read ↗

Expression of mutant α1 Na/K-ATPase defective in conformational transition attenuates Src-mediated signal transduction.Semantic proximity Read ↗

Differential regulation of renal Na,K-ATPase by splice variants of the gamma subunit.Semantic proximity Read ↗

Intracellular localization of Na,K-ATPase alpha2 subunit mutants.Semantic proximity Read ↗

The structure of the Na+,K+-ATPase and mapping of isoform differences and disease-related mutations.Semantic proximity Read ↗

Functional expression of rat alpha 1 Na,K-ATPase containing substitutions for cysteines 454, 458, 459, 513 and 551.Semantic proximity Read ↗

Isoforms of the Na,K-ATPase: family members in search of function.Semantic proximity Read ↗

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