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Published in Science Advances, co-corresponding author Ravi Kalathur, PhD, St. Jude Protein Technologies Center director, structurally characterized ERMA, a key player in magnesium regulation in cells.
A newly discovered ATPase regulates magnesium ion levels in the endoplasmic reticulum
Ion transport plays an essential role in virtually all cellular processes. Although sodium, potassium, calcium and hydrogen ion P-type ATPase transporters are well studied, magnesium ion P-type ATPase transporters remain poorly understood. Published in Science Advances, scientists from St. Jude Children’s Research Hospital, University of Texas Health Science Center at San Antonio and the University of Texas Southwestern Medical Center investigated ERMA, a protein that transports magnesium ions across the endoplasmic reticulum membrane. The researchers found that ERMA has a typical P-type ATPase fold, with some key structural variations.
The multi-institute team, including co-first author Michael Oldham, PhD, St. Jude Department of Structural Biology, discovered that ERMA serves as a gatekeeper to a magnesium ion reservoir within the endoplasmic reticulum.
The study also reveals how ERMA serves as a gatekeeper to a magnesium ion reservoir within the endoplasmic reticulum, expanding scientists’ understanding of this organelle’s cellular roles, which also includes calcium storage, protein synthesis and lipid metabolism.
“More than 90% of the ATP in our cells is bound to magnesium ions, and this ATP-magnesium pair is the energy source for all ATP-dependent processes in our body. Therefore, it is crucial that cells keep the levels of free magnesium low; ERMA is a key player in this balancing act,” said co-corresponding author Ravi Kalathur, PhD, St. Jude Protein Technologies Center director. “There are diseases associated with magnesium dysregulation, and the fundamental structural and functional understanding that we have uncovered may help find new treatments for these diseases.”