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

Amino acids Lys-Asp-Asp-Lys-Pro-Val402 in the Ca(2+)-ATPase of cardiac sarcoplasmic reticulum are critical for functional association with phospholamban.

The Journal of biological chemistry - 16 Sept 1994

Toyofuku T, Kurzydlowski K, Tada M, MacLennan D H

Abstract excerpt

Phospholamban interacts with SERCA2 (sarco/endoplasmic reticulum calcium ATPase isoform 2) but not SERCA3. The use of chimeric SERCA2/SERCA3 molecules has revealed that amino acids 336-412 in the phosphorylation domain of SERCA2 are essential for functional association with phospholamban (Toyofuku, T., Kurzydlowski, K., Tada, M., and MacLennan, D. H. (1993) J. Biol. Chem. 268, 2809-2815). When mutations were made...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Binding Sites

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

Share to Molecular Sequence Data

Share to Mutation

Share to Myocardium

Share to Peptide Fragments

Share to Rabbits

Share to Recombinant Fusion Proteins

Source

Identifiers

PMID: 8083189

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

Amino acids Lys-Asp-Asp-Lys-Pro-Val402 in the Ca(2+)-ATPase of cardiac sarcoplasmic reticulum are critical for functional association with phospholamban.PMID 8083189Read ↗

Transmembrane helix M6 in sarco(endo)plasmic reticulum Ca(2+)-ATPase forms a functional interaction site with phospholamban. Evidence for physical interactions at other sites.Semantic proximity Read ↗

The SERCA residue Glu340 mediates interdomain communication that guides Ca2+ transport.Semantic proximity Read ↗

Functional and physical competition between phospholamban and its mutants provides insight into the molecular mechanism of gene therapy for heart failure.Semantic proximity Read ↗

Phosphorylation and mutation of phospholamban alter physical interactions with the sarcoplasmic reticulum calcium pump.Semantic proximity Read ↗

Sarco(endo)plasmic reticulum calcium pumps: recent advances in our understanding of structure/function and biology (review).Semantic proximity Read ↗

Hydrophobic imbalance in the cytoplasmic domain of phospholamban is a determinant for lethal dilated cardiomyopathy.Semantic proximity Read ↗

Role of leucine 31 of phospholamban in structural and functional interactions with the Ca2+ pump of cardiac sarcoplasmic reticulum.Semantic proximity Read ↗

Tuning the structural coupling between the transmembrane and cytoplasmic domains of phospholamban to control sarcoplasmic reticulum Ca(2+)-ATPase (SERCA) function.Semantic proximity Read ↗

Sarcolipin protein interaction with sarco(endo)plasmic reticulum Ca2+ ATPase (SERCA) is distinct from phospholamban protein, and only sarcolipin can promote uncoupling of the SERCA pump.Semantic proximity Read ↗

A phospholamban-tethered cardiac Ca2+ pump reveals stoichiometry and dynamic interactions between the two proteins.Semantic proximity Read ↗

Identification of Ser38 as the site in cardiac sarcoplasmic reticulum Ca(2+)-ATPase that is phosphorylated by Ca2+/calmodulin-dependent protein kinase.Semantic proximity Read ↗

Dissection of the functional differences between sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) 1 and 2 isoforms and characterization of Darier disease (SERCA2) mutants by steady-state and transient kinetic analyses.Semantic proximity Read ↗

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