Phosphorylated proteins in Drosophila membranes.
Reversible protein modification-demodification in bacterial membranes has been shown to be an important mechanism for the adaptive behavior of bacteria in response to chemosensory stimuli. It has been suggested that the protein modification mechanisms might have wider functional implications and might form the basis for an understanding of complex phenomena such as information storage and retrieval. Phosphorylation of membrane proteins in the mammalian system is a well-documented phenomenon. Greengard and coworkers have shown that phosphorylation of a set of synaptic membrane proteins, collectively known as protein I is stimulated specifically in response to cAMP and calcium. We have explored the possibility of in vitro phosphorylation of proteins in membrane preparations obtained from Drosophila fly heads. Here we present a preliminary report of these studies.
D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002458:Cell Fractionation / Q000379:methods; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure; D000242:Cyclic AMP / Q000494:pharmacology; D004331:Drosophila melanogaster / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D008970:Molecular Weight; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation
D008565:Membrane Proteins; D010750:Phosphoproteins; D000242:Cyclic AMP; D002118:Calcium