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Searching For Binding Partners For The Novel Phkg1 Variant, Phkγ 181, Kishore Polireddy
Searching For Binding Partners For The Novel Phkg1 Variant, Phkγ 181, Kishore Polireddy
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Phopshorylase kinase (PhK) is a hexadecameric holoenzyme made up of four different subunits in the arrangement (αβγδ)4 and has total molecular mass of 1.3MDa. Alpha and β are regulatory subunits, γ is catalytic, and δ is an intrinsic molecule of calmodulin. PhK is a serine threonine kinase with glycogenolytic regulatory functions. Our lab has recently discovered that the γ subunit can be alternatively processed to produce a truncated form of 181 residues (γ-181). This variant of γ contains a phosphorylation site for PK-C, and its activity is influenced by this phosphorylation. We are using a LexA based yeast two hybrid …