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Review
. 2022 Aug 30:10:992235.
doi: 10.3389/fcell.2022.992235. eCollection 2022.

Calcium in peroxisomes: An essential messenger in an essential cell organelle

Affiliations
Review

Calcium in peroxisomes: An essential messenger in an essential cell organelle

Yelena Sargsyan et al. Front Cell Dev Biol. .

Abstract

Calcium is a central signal transduction element in biology. Peroxisomes are essential cellular organelles, yet calcium handling in peroxisomes has been contentious. Recent advances show that peroxisomes are part of calcium homeostasis in cardiac myocytes and therefore may contribute to or even shape their calcium-dependent functionality. However, the mechanisms of calcium movement between peroxisomes and other cellular sites and their mediators remain elusive. Here, we review calcium handling in peroxisomes in concert with other organelles and summarize the most recent knowledge on peroxisomal involvement in calcium dynamics with a focus on mammalian cells.

Keywords: Ca2+; FRET sensor; calcium; cardiomyocyte; cell organelle; peroxisomes.

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Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

FIGURE 1
FIGURE 1
Peroxisomal Calcium—an Overview. In mammalian cells, cytosolic Ca2+ levels are around 100 nM, whereas the endoplasmic reticulum (ER) as a main cellular Ca2+ store has several hundred micromolar Ca2+ (Samtleben et al., 2013). An average peroxisome contains around 600 nM Ca2+ (Sargsyan et al., 2021). Ca2+ likely enters peroxisomes either through a channel/pore or a transporter (Ch). The entry and exit mechanism of Ca2+, however, may differ (T1/T2 hypothetical importer/exporter). Known protein tethers form contact sites (CS) between peroxisomes and the ER, potentially create microdomains that facilitate the exchange of Ca2+. Ca2+ may bind to a yet unknown intraperoxisomal protein (P) or membrane protein and affect its function, e.g., by inducing a conformational change when bound to Ca2+. Hypothetical elements of the model (channel, transporter, intraperoxisomal Ca2+-sensitive protein) are shown in gray.

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