Calmodulin at the channel gate

Article Abstract:

Calmodulin, the classical Ca2+ receptor protein inside cells, has been found to mediate both inactivation and facilitation. Mutant forms of calmodulin, which are unable to bind Ca2+, act as dominant-negative inhibitors of Ca2+-channel inactivation. A number of biochemical strategies have indicated that calmodulin binds to the IQ motif of the L-type Ca2+ channel. Ca2+ both inactivates and facilitates Ca2+ channels by binding to calmodulin, with both processes involving binding of CA2+-calmodulin to the IQ motif.

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Competitive binding of alpha-actinin calmodulin to the NMDA receptor

Article Abstract:

A functionally significant relationship between N-methyl-D-aspartate (NMDA) receptors and the postsynaptic cytoskleton is indicated by the mechano-sensitivity of these receptors and by their dependence on the integrity of actin. There are indications that the localization of NMDA receptors and their moderation by Ca2+/calmodulin are influenced by actin-binding protein alpha-actinin-2.

Protein binding, Neurotransmitter receptors, Methyl aspartate, N-methyl-D-aspartate

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Ca(super 2+)/calmodulin is critical for brassinosteroid biosynthesis and plant growth

Article Abstract:

Study is conducted to show that Arabidopsis DWARF1 (DWF1) is a Ca(super 2+)/calmodulin-binding protein and this binding is critical for its function of brassinosteroid biosynthesis and plant growth. The results raise the possibility of producing size-energized crops by altering the Ca(super 2+)/calmodulin property of their DWF1 orthologues.

Science & research, Plants, Plant development, Plant molecular genetics

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