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Using InCELLect™ Peptides to Probe PKC-Mediated Cellular Signaling Reaction In Vivo

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Abstract

Protein kinase- and phosphatase-mediated phosphorylation and dephosphorylation are key mechanisms used in cellular regulation. In addition to activation, precise subcellular localization is required for signaling specificity in response to a stimulus. Protein-protein interaction facilitates appropriate associations among members of a signaling cascade, which can be in the form of a scaffold or an anchor. Peptides derived from anchoring proteins can disrupt the interaction  between enzymes and their anchoring proteins. A peptide derived from the A Kinase-Anchoring Protein (AKAP) Ht-31 (human thyroid) disrupts A kinase anchoring and thus A kinase-mediated responses in several model systems.

We have generated stearated forms of the peptide, InCELLect™ AKAP St-Ht31 (Cat,# V8211), and its corresponding control peptide, InCELLect™ St-Ht31P (Cat.# V8221), which are cell permeable and facilitate the study of AKAP in mediating PKA responses. This article describes recent research using Promega's stearated peptides-InCELLect™ AKAP St-Ht31 Inhibitor Peptide and InCELLect™ St-Ht31P Control Peptide--on PKA anchoring in the cell.

Promega Notes 75, 29–32.

Said Goueli and Kevin Hsaio

Promega Corporation
Publication Date: 2000

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