Protein kinase C in larval brain of wild-type and dunce memory-mutant Drosophila.
Protein kinase C activity has been measured in extracts of larval brain of Drosophila melanogaster, with the synthetic nonapeptide substrate Ala-Ala-Ala-Ser-Phe-Lys-Ala-Lys-Lys-amide. Protein kinase C activity in such extracts is abolished in a Ca2+-dependent manner at 18 degrees C, and partly converted to a form independent of effectors. The decay of protein kinase C activity can be prevented by leupeptin or a crude calpastatin preparation isolated from fly heads, indicating the presence of the Ca2+-dependent neutral protease, calpain, in larval brains. The total protein kinase C levels were nearly the same in wild type and three different dunce "memory-mutant" strains. In contrast, the soluble/particulate activity ratios were different: wild-type, 0.91; dunce M11, 0.46; dunce M11/Df(1)dm75e19, 1.23; dunce2, 0.88. These data suggest that the membrane adherence of protein kinase C in larval brain is governed by the actor of genes other than dunce.
Dévay
P
P
Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest.
Pintér
M
M
Kiss
I
I
Faragó
A
A
Friedrich
P
P
D000818:Animals; D001921:Brain / Q000201:enzymology / Q000502:physiology; D004331:Drosophila melanogaster / Q000201:enzymology / Q000235:genetics* / Q000502:physiology; D007700:Kinetics; D007814:Larva; D008568:Memory; D009154:Mutation; D011493:Protein Kinase C / Q000378:metabolism*
D011493:Protein Kinase C