TRPM7 is a bifunctional protein consisting of a cation channel fused to a kinase domain. TRPM7 plays a variety of roles in the cell, including cell proliferation, cytoskeletal organization and embryonic development. Recent studies suggest that TRPM7 is involved in the proliferation of cancer cells.While the channel properties of TRPM7 have been studied extensively, little is known about the mechanisms regulating its kinase activity. The Rapid Quench Flow Kinetic study of its autophosphorylation and autoactivation revealed that the first three phosphates added to the enzyme are enough to make the enzyme fully active against its substrates When we tested alanine mutation of those early phosphorylation sites, all of them showed almost no activity. TRPM7 alanine mutants did not interact with myosin IIB suggesting that the interaction between TRPM7 and myosin IIB requires an active kinase domain. In conclusion, three early autophosphosphorylations of TRPM7 regulate its autoactivity and myosin IIb binding.

Three early autophosphosphorylations of TRPM7 regulate its autoactivity and myosin IIB binding

245th National Meeting (2013)

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