Abstract
Protein Kinase C δ (δPKC)-Annexin V Interaction: A REQUIRED STEP IN δPKC TRANSLOCATION AND FUNCTION
Highlights
Protein-protein interactions determine the specificity of many cellular signaling events
This intramolecular interaction is broken upon Protein kinase C (PKC) activation, allowing PKC binding to its RACK
We found that ␦PKC-annexin V interaction precedes ␦PKC translocation to the cell particulate fraction and that microtubule integrity and energy are required for the dissociation of the complex
Summary
Protein-protein interactions determine the specificity of many cellular signaling events. One set of such interactions is mediated by RACKs2 (receptors for activated C-kinase) that localize different activated protein kinase C (PKC) isozymes to distinct subcellular sites and determine isozyme-specific roles by anchoring each active PKC next to its corresponding substrates [1]. Though much is known about its downstream signaling events, the process of ␦PKC translocation and activation, and the proteins that regulate it have not been identified. We do not have access to JTV-519 for this study, based on the observations described above, we hypothesized that annexin V plays a role in the ␦PKC translocation process
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