Calcium-dependent levels of phospholamban pentamer in native heart membranes reflect interactions of monomers with calcium-free SERCA2a
We have developed a simple, effective method and revealed that the levels of SERCA2a inhibition are controlled by an equilibrium between PLB<sub>1</sub> association with E2 and its dissociation from E1, and the formation of PLB<sub>5</sub> in native cardiac SR membranes. With intact regulatory components in their natural phospholipid environment, Ca<sup>2+</sup>-dependent shifts in PLB<sub>5</sub>/PLB<sub>1</sub> can expose PLB-SERCA2a protein-protein interactions in native membranes from normal and diseased hearts, in which proteomes and lipidomes are likely to vary.
Authors
- Jin Guo (ORCID: https://orcid.org/0000-0002-0093-1927)
- Zhenhui Chen (ORCID: https://orcid.org/0000-0002-1781-5332)
- Kazuhiro Aonuma
- Richard Kovacs
Institutions
- Indiana University Health (US)
- University of Indianapolis (US)
- Indiana University – Purdue University Indianapolis (US)
Publication Details
- Journal
- Archives of Biochemistry and Biophysics
- Published
- 2025-04-20
- DOI
- https://doi.org/10.1016/j.abb.2025.110432
- Primary Topic
- Cardiac electrophysiology and arrhythmias
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- American Heart Association
- National Institutes of Health