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Signal Transduction and Protein Phosphorylation (Paperback, Softcover reprint of the original 1st ed. 1987)
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Signal Transduction and Protein Phosphorylation (Paperback, Softcover reprint of the original 1st ed. 1987)
Series: NATO Science Series A:, 135
Expected to ship within 10 - 15 working days
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A NATO Advanced Study Institute on "Signal Transduction and Protein
Phosphorylation" was held to overview recent developments in this
area. The participants in the Institute dealt with protein
phosphorylation as the most prevalent mode of regulation of
cellular processes. First, methods needed to analyze the complex
cascade systems involved were reviewed, including protein
sequencing, crystallo- graphy, characterization and isolation of
membrane proteins, use of monoclonal or polyclonal antibodies and
application of fluorescent probes. In great detail the x ray
crystallographic structure of glycogen phosphorylase was presented.
This enzyme is located at the end of a signal cascade triggered by
the hormonal activation of the membrane-bound adenylate cyclase.
The interaction of the hormone/receptor with the catalytic subunit
of the adenylate cyclase involves GTP-binding proteins. The
function of these recently detected intermembrane coupling factors
were reviewed, as weIl as the structure and properties of various
protein kinases. 2 Major emphasis was placed on Ca + as a second
messenger, its metabolism, mechanism of release and uptake from
intracellular stores and its role on cell motility and muscle
contraction. Two classes of protein phosphatases were discussed.
They differ in their subunit structure and substrate specificity
and are subject of a highly complex regulatory mechanism as yet not
fully under- stood.
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