Phosphorylated Proteins in Drosophila Membranes

  • Pallaiah Thammana
Part of the Basic Life Sciences book series (BLSC, volume 16)


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.1 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.1,2 Phosphorylation of membrane proteins in the mammalian system is a well-documented phenomenon.3 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.2–4 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.


Membrane Fraction Lated Membrane Protein Phosphorylation Reaction Crude Membrane Fraction Cold Spring Harbor Symposium 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    M.S. Springer, M.F. Goy and J. Adler, Protein methylation in behavioral control mechanisms and in signal transduction, Nature, 280: 279 (1979).PubMedCrossRefGoogle Scholar
  2. 2.
    P. Greengard, Possible role for cyclic nucleotides and phosphorylated membrane proteins in postsynaptic actions of neurotransmitters, Nature, 260: 101 (1976).PubMedCrossRefGoogle Scholar
  3. 3.
    T. Ueda and P. Greengard, Adenosine 3’:5’-monophosphate-regulated phosphoprotein system of neuronal membranes, J. Biol. Chem., 252: 5155 (1977)PubMedGoogle Scholar
  4. 4.
    W.B. Huttner and P. Greengard, Multiple phosphorylation sites in protein I and their differential regulation by cyclic AMP and calcium, Proc. Natl. Acad. Sci., U.S.A., 76: 5402 (1979).PubMedCrossRefGoogle Scholar
  5. 5.
    T.R. Venkatesh, S. Zingde and K.S. Krishnan, Isolation and characterization of membranes from Drosophila melanogaster,this volume.Google Scholar
  6. 6.
    P.H. O’Farrell, High resolution two-dimensional electrophoresis of proteins, J. Biol. Chem., 250: 4007 (1975).PubMedGoogle Scholar
  7. 7.
    A. Martonosi, R. Boland and R.A. Halpin, The biosynthesis of sarcoplasmic reticulum membranes and the mechanism of calcium transport, Cold Spring Harbor Symposia on Quantitative Biology, 32: 455 (1972).Google Scholar
  8. 8.
    D.H. MacLennan, C.C. Yip, G.H. Iles and P. Seeman, Isolation of sarcoplasmic reticulum proteins, Cold Spring Harbor Symposia on Quantitative Biology, 32: 469 (1972).Google Scholar

Copyright information

© Springer Science+Business Media New York 1980

Authors and Affiliations

  • Pallaiah Thammana
    • 1
  1. 1.Tata Institute of Fundamental ResearchBombayIndia

Personalised recommendations