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Immunocytochemical Localization and Crystal Structure of Human Frequenin (Neuronal Calcium Sensor 1)

Abstract : Frequenin, a member of a large family of myristoylswitch calcium-binding proteins, functions as a calciumion sensor to modulate synaptic activity and secretion. We show that human frequenin colocalizes with ARF1 GTPase in COS-7 cells and occurs in similar cellular compartments as the phosphatidylinositol-4-OH kinase PI4K␤, the mammalian homolog of the yeast kinase PIK1. In addition, the crystal structure of unmyristoylated, calcium-bound human frequenin has been determined and refined to 1.9 Å resolution. The overall fold of frequenin resembles those of neurocalcin and the photoreceptor, recoverin, of the same family, with two pairs of calcium-binding EF hands and three bound calcium ions. Despite the similarities, however, frequenin displays significant structural differences. A large conformational shift of the C-terminal region creates a wide hydrophobic crevice at the surface of frequenin. This crevice, which is unique to frequenin and distinct from the myristoyl-binding box of recoverin, may accommodate a yet unknown protein ligand.
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https://hal-amu.archives-ouvertes.fr/hal-03263149
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Yves Bourne, Jens Dannenberg, Verena Pollmann, P. Marchot, Olaf Pongs. Immunocytochemical Localization and Crystal Structure of Human Frequenin (Neuronal Calcium Sensor 1). Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2000, 276, pp.11949 - 11955. ⟨10.1074/jbc.m009373200⟩. ⟨hal-03263149⟩

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