TRPM7: Difference between revisions

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Latest revision as of 03:00, 18 March 2025

TRPM7 is a member of the transient receptor potential channels (TRP channels) family, which are a group of ion channels located mostly on the plasma membrane of numerous animal cell types. The TRPM7 channel is a significant component of cellular magnesium homeostasis and is involved in various cellular processes.

Structure[edit]

TRPM7 is a fusion protein that consists of an ion channel domain and an alpha-kinase domain. The ion channel domain is located at the N-terminus of the protein, while the alpha-kinase domain is located at the C-terminus. The ion channel domain is responsible for the permeability of the channel to divalent cations, including magnesium and calcium.

Function[edit]

TRPM7 plays a crucial role in cellular magnesium homeostasis. It is a non-selective cation channel that is permeable to divalent cations, including magnesium and calcium. The channel is constitutively active, meaning it is always open under physiological conditions. The alpha-kinase domain of TRPM7 has been shown to phosphorylate a variety of substrates, including myosin II, annexin I, and the TRPM7 channel itself.

Clinical Significance[edit]

Mutations in the TRPM7 gene have been associated with several diseases, including Guillain-Barré syndrome, anoctamin 5-related myopathy, and hypomagnesemia. In addition, TRPM7 has been implicated in the pathogenesis of various types of cancer, including breast, pancreatic, and colon cancer.

See Also[edit]

References[edit]

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