Phosphorylation of lipocortins in vitro by protein kinase C

Khanna, Navin C. ; Tokuda, Masaaki ; Waisman, David M. (1986) Phosphorylation of lipocortins in vitro by protein kinase C Biochemical and Biophysical Research Communications, 141 (2). pp. 547-554. ISSN 0006-291X

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Protein kinase C catalyzes the incorporation of about 1.1, 0.7 and 0.4 mole of phosphate per mole of Lipocortin-I (P35), Lipocortin-II (P36) and Lipocortin-85 (P36 oligomer) respectively. The phosphorylation is specific for protein kinase C and is dependent on the presence of both calcium and phospholipids. While Lipocortin-I is phosphorylated on threonine residues, Lipocortin-II and Lipocortin-85 are phosphorylated on serine residues.The substoichiometric phosphorylation of Lipocortin-85 appears to preclude the potential regulation of this protein by protein kinase C. The phosphorylation of Liporcortin-I on threonine residues and Lipocortin-II on serine residues suggests these proteins may be regulated by distinct phosphorylation dephosphorylation reactions.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
ID Code:109132
Deposited On:09 Mar 2018 12:14
Last Modified:09 Mar 2018 12:14

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