Download Biological Signal Transduction by Jean-Luc Galzi, Jean-Pierre Changeux (auth.), Elliott M. PDF

By Jean-Luc Galzi, Jean-Pierre Changeux (auth.), Elliott M. Ross, Karel W. A. Wirtz (eds.)

Offering a survey on present learn in eukaryotic sign transduction, many of the subject matters lined are, the biochemistry and biophysics of mobilephone floor receptors, G-protein mediated signalling pathways, law of cyclic AMP, Ca2+, inositol phosphate pathways, the constitution and legislation of receptors that are tyrosine protein kinases, and mobile responses to built-in signs.

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In previous reports, we and others interpreted the appearance of the -360 kOa as to represent the proces of receptor dimerization. However our findings and those of others are also consistent with the possibility that the EGF-induced -360 kOa band represents preexisting EGF receptor dimers which can only be trapped by crosslinking upon binding of EGF. In this respect, very recently, interesting experiments have been preformed with truncated EGF receptors which were only expressed at the cell surface if wild type 37 receptors were present.

Cell 41 :719-726 Prywes R, Livneh E, Ullrich A, Schlessinger J (1986) Mutations in the cytoplasmic domain of EGF receptor affect EGF binding and receptor internalization. EMBO J 5:2179-2190 Raines MA, Maihle NJ, Moscovici C, Moscovici MG, Kung HJ (1988) Molecular characterization of three erbB transducing viruses generated during ALV induced erythroleukemia: Extensive internal deletion near the kinase domain activates the fibrosarcoma and hemangioma-inducing potential of erbB. J Viml 62:2444-2452 Riedel H, Schlessinger J, Ullrich A (1987) A chimeric, ligand-binding v-erbB/EGF receptor retains transforming potential.

It is conceivable that the electric field across the plasma membrane may act on charged residues of the receptor located near the inner side of the plasma membrane or that it may modulate putative noncovalent interactions that could be important for dimer stabilization. To test the possible effects of alterations in transmembrane potential, dimer stabilization was followed in cells incubated in medium containing 150 mM K+, which abolishes the transmembrane potential. However in vivo stabilization of dimers in this high K+ buffer was comparable to control, 36 indicating that the electric field across the plasma membrane is not important for receptor dimer stabilization.

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