Publications by authors named "Ashkan Shahsavan"
Article Synopsis
- Cystathionine- -synthase (CBS)-pair domain transporters (CNNMs) are important for regulating magnesium levels in the body by transporting magnesium ions and affecting a specific ion channel (TRPM7).
- The study presents the crystal structure of the extracellular part of tapeworm CNNM4, revealing it forms a dimer with specific molecular structures and sites for sugar molecules.
- Mutations in the extracellular domain of human CNNM4 hinder its dimerization, and a similar mutation in mouse CNNM2 negatively affects its ability to transport magnesium in cells.
Cystathionine-β-synthase (CBS)-pair domain divalent metal cation transport mediators (CNNMs) are an evolutionarily conserved family of magnesium transporters. They promote efflux of Mg ions on their own and influx of divalent cations when expressed with the transient receptor potential ion channel subfamily M member 7 (TRPM7). Recently, ADP-ribosylation factor-like GTPase 15 (ARL15) has been identified as CNNM-binding partner and an inhibitor of divalent cation influx by TRPM7.
View Article and Find Full Text PDFCystathionine-β-synthase (CBS)-pair domain divalent metal cation transport mediators (CNNMs) are an evolutionarily conserved family of magnesium transporters. They promote efflux of Mg ions on their own or uptake of divalent cations when coupled to the transient receptor potential ion channel subfamily M member 7 (TRPM7). Recently, ADP-ribosylation factor-like GTPase 15 (ARL15) has been identified as CNNM binding partner and an inhibitor of divalent cation influx by TRPM7.
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