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Science 19 December 1997: Vol. 278. no. 5346, pp. 2075 - 2080 DOI: 10.1126/science.278.5346.2075
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Articles
Signaling Through Scaffold, Anchoring, and Adaptor Proteins
Tony Pawson,
John D. Scott
The process by which extracellular signals are relayed from the
plasma membrane to specific intracellular sites is an essential facet
of cellular regulation. Many signaling pathways do so by altering the
phosphorylation state of tyrosine, serine, or threonine residues of target proteins. Recently, it has become apparent that
regulatory mechanisms exist to influence where and when protein kinases
and phosphatases are activated in the cell. The role of scaffold,
anchoring, and adaptor proteins that contribute to the specificity of
signal transduction events by recruiting active enzymes into signaling
networks or by placing enzymes close to their substrates is discussed.
T. Pawson is at the Samuel Lunenfeld Research Institute, Mount
Sinai Hospital, Toronto, Ontario M5G 1X5, Canada. J. D. Scott,
Howard Hughes Medical Institute, Vollum Institute, Portland, OR
97201-3098, USA.
Read the Full Text
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Physiol Genomics
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- Stable Isotope Labeling with Amino Acids in Cell Culture (SILAC) for Studying Dynamics of Protein Abundance and Posttranslational Modifications.
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- The 15-Amino Acid Motif of the C Terminus of the {beta}2-Adrenergic Receptor Is Sufficient to Confer Insulin-Stimulated Counterregulation to the {beta}1-Adrenergic Receptor.
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- The Luteinizing Hormone-releasing Hormone Inhibits the Anti-apoptotic Activity of Insulin-like Growth Factor-1 in Pituitary {alpha}T3 Cells by Protein Kinase C{alpha}-mediated Negative Regulation of Akt.
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