Molecular glue: kinase anchoring and scaffold proteins
Article Abstract:
Research in protein kinase and phosphatase genes indicates that cellular event control is facilitated by the formation of kinase-phosphatase signaling complexes. The control of these complexes is effected by the manner in which adapter proteins act as platforms for signal unit assembly. 'Scaffold' proteins attract several kinases of a signal pathway and regulate the action of each kinase in a sequential manner for a single control event. 'Anchoring' proteins attract a few kinase or phosphatase close to their specific substrates and take signals from the attached enzymes that control several activities.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
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Protein kinase C as a molecular machine for decoding calcium and diacylglycerol signals
Article Abstract:
A molecular mechanism which guarantees that conventional protein kinase C (PKC) isoforms are sequentially activated by calcium and diacylglycerol signals was discovered. It was shown that GFP-tagged PKC-gamma translocated to the plasma membrane in response to hormonal stimuli. The translocation of C2-GFP was regulated by calcium and the translocation of C1(sub-2)-GFP by diacylglycerol. The properties of the molecular mechanism make PKC-gamma responsive to persistent diacylglycerol increases combined with high- but not low-frequency calcium spikes.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
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LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation
Article Abstract:
Research was conducted to describe the cloning of the cDNA for a highly tyrosine-phosphorylated 36-38 kDA protein and characterize a linker for activation of T cells (LAT) as a substrate of activated ZAP-70. The calcium phosphate method was utilized to carry out the transfection of 293T cells. Results showed that the amino acid sequence was characterized by a hydrophobic region near the amino acid terminus and that LAT can be expressed in Jurkat T cells as two forms.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
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