Document Type
Article
Publication Date
11-11-2025
Abstract
In adult cardiomyocytes, within the Mitochondrial Associated Membranes (MAMs), the sarcoplasmic reticulum (SR) and mitochondria juxtapose each other, forming a unique and highly repetitive functional structure throughout the cells. These SR-mitochondria contact sites have emerged as critical structures that regulate various physiological processes, including lipid exchange, calcium (Ca2+) communication, control of excitation-contraction bioenergetics coupling, and reactive oxygen species (ROS) production. Over the years, several scientific studies have reported the accumulation of diverse proteins within these SR-mitochondria close contacts. Some proteins strategically accumulate in these areas to enhance their function, such as the mitochondrial Ca2+ uniporter, while others perform non-canonical roles, such as DRP1 acting as a bioenergetics regulator. The purpose of this review is to provide a comprehensive compilation of the proteins that have been reported to be enriched in cardiac MAMs. We aim to show how their positioning is crucial for proper cardiac physiology and fitness, as well as how mispositioning may contribute to cardiac diseases. Additionally, we will discuss the gaps in our understanding and identify the necessary components to fully comprehend physiological communication between the sarcoplasmic SR and mitochondria in cardiac tissue.
Recommended Citation
Fernandez-Sanz, Celia; Sheu, Shey-Shing; and De La Fuente, Sergio, "Cardiac SR-Mitochondria Contacts-Impact on Cardiac Physiology and Mitochondrial Fitness" (2025). Center for Translational Medicine Faculty Papers. Paper 139.
https://jdc.jefferson.edu/transmedfp/139
Creative Commons License

This work is licensed under a Creative Commons Attribution 4.0 License.
PubMed ID
41294815
Language
English


Comments
This article is the author’s final published version in Cells, Volume 14, Issue 22, 2025, Article number 1762.
The published version is available at https://doi.org/10.3390/cells14221762. Copyright © 2025 by the authors.