title: Identification and characterization of MARCKS in Xenopus laevis.
abstract: MARCKS proteins are widely distributed in mammalian cells and subserve an important role as probes in the examination of signal transduction processes because they are specific endogenous phosphoreceptors for activated protein kinase C. Experiments were performed to determine whether MARCKS proteins are present in amphibia and to show their usefulness as substrates for stimulated PKC activation, using cultured renal epithelial cells (A6) derived from Xenopus laevis as an experimental model.
authors.affiliation: Department of Internal Medicine, Yale School of Medicine, New Haven, Connecticut 06510, USA.
authors.forename: N
authors.initials: N
authors.lastname: Ali
authors.forename: L J
authors.initials: LJ
authors.lastname: Macala
authors.forename: J P
authors.initials: JP
authors.lastname: Hayslett
mesh_terms: D000818:Animals; D002478:Cells, Cultured; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D015151:Immunoblotting; D047908:Intracellular Signaling Peptides and Proteins; D007668:Kidney; D008565:Membrane Proteins; D008970:Molecular Weight; D000076250:Myristoylated Alanine-Rich C Kinase Substrate; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism*; D011506:Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology; D014667:Vasopressins / Q000494:pharmacology; D014982:Xenopus laevis
chemical_list: D047908:Intracellular Signaling Peptides and Proteins; D008565:Membrane Proteins; D011506:Proteins; D014667:Vasopressins; D000076250:Myristoylated Alanine-Rich C Kinase Substrate; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate