Abstract
Screening for protein interaction partners of ion channels helps to elucidate signaling cascades to cellular targets and processes for a better understanding of the origin of diseases. Most important are the cytosolic segments of membrane- bound voltage- and ligand-gated ion channels or from ion channel regulators, which may connect to specific signaling complexes. So far, not much is known about those interactions. Molecular chaperones are proteins, which support the biosynthesis of proteins during maturation without being part of the final protein complex or which support the degradation of targeted proteins within the cellular protein quality control.
Keywords: Protein-protein interaction, ion channel signaling cascades, neurodegeneration
Current Pharmaceutical Biotechnology
Title: Heat Shock Proteins and Ion Channels. Functional Interactions and Therapeutic Consequences
Volume: 11 Issue: 2
Author(s): Kayalvizhi Radhakrishnan, Jurgen Hescheler and Toni Schneider
Affiliation:
Keywords: Protein-protein interaction, ion channel signaling cascades, neurodegeneration
Abstract: Screening for protein interaction partners of ion channels helps to elucidate signaling cascades to cellular targets and processes for a better understanding of the origin of diseases. Most important are the cytosolic segments of membrane- bound voltage- and ligand-gated ion channels or from ion channel regulators, which may connect to specific signaling complexes. So far, not much is known about those interactions. Molecular chaperones are proteins, which support the biosynthesis of proteins during maturation without being part of the final protein complex or which support the degradation of targeted proteins within the cellular protein quality control.
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Cite this article as:
Radhakrishnan Kayalvizhi, Hescheler Jurgen and Schneider Toni, Heat Shock Proteins and Ion Channels. Functional Interactions and Therapeutic Consequences, Current Pharmaceutical Biotechnology 2010; 11 (2) . https://dx.doi.org/10.2174/138920110790909678
DOI https://dx.doi.org/10.2174/138920110790909678 |
Print ISSN 1389-2010 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4316 |
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