Area:
Neuroscience Biology, General Biophysics, Pharmacology
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High-probability grants
According to our matching algorithm, Peter H. Reinhart is the likely recipient of the following grants.
Years |
Recipients |
Code |
Title / Keywords |
Matching score |
1993 — 2000 |
Reinhart, Peter H |
R01Activity Code Description: To support a discrete, specified, circumscribed project to be performed by the named investigator(s) in an area representing his or her specific interest and competencies. R29Activity Code Description: Undocumented code - click on the grant title for more information. |
Neuromodulation of Ion Channels
Ion channels are not simply passive pores, but are dynamic entities subject to modulation that can last for seconds, minutes, or even hours. I propose to investigate the mechanisms by which the phosphorylation of ion channels produces such long-term modulation. In particular I will examine whether ion channels can exist as regulatory complexes tightly associated with modulatory proteins. The study will focus on a group of large conductance Ca2+-activated K+ channels from rat brain, because many of these channels can be modulated by phosphorylation of either the channel itself, or of closely associated proteins. The specific aims are: 1) to explore whether ion channels can reside in membranes as protein complexes, tightly associated with regulatory components such as protein kinases and protein phosphatases; 2) to examine the contribution of individual phosphorylation sites on the gating of ion channels that are multiply phosphorylated; 3) to investigate the interactions between different protein kinases that act on a single ion channel; and 4) to define the role and specificity of protein phosphatases in modulating channel gating. These experiments will rely on two complementary experimental approaches. First, planar lipid bilayers will be used to reconstitute individual ion channels separated from all cytoplasmic influences. The effect of purified protein kinases and phosphatases on channel gating will be examined. Second, channel modulation in native membranes and intact cells will be investigated by patch-clamping cultured neurons. While there is much descriptive information about how neurons respond to extracellular signals by an alteration in their electrical activity, little is known about the mechanisms by which these modulators alter channel gating. This work will aim to provide such mechanistic information, particularly in the context of ion channel / kinase phosphatase complexes. Such complexes may represent a common target for multiple second messenger pathways, and play a role in the integration, and perhaps even the storage, of information carried by extracellular signals.
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1 |
2001 — 2004 |
Reinhart, Peter H |
R01Activity Code Description: To support a discrete, specified, circumscribed project to be performed by the named investigator(s) in an area representing his or her specific interest and competencies. |
Calcium Activated K+ Channels in Brain
DESCRIPTION (provided by applicant): A single class of proteins - the ion channels - is the major determinant of neuronal signaling properties, and a long-term objective of this laboratory is to determine the contributions made by individual classes of ion channel to the signaling properties of neurons. Our current focus is on a family of K+ channels, the Ca2+-activated potassium channels because 1) they are found in virtually all neurons and also in many non-neuronal cells, 2) they play numerous functional roles in these various cell types, and 3) the properties of these channels varies in different cellular contexts due to the association of hetero-tetramers, alternative splicing, association with other accessory proteins, and modulation by second messenger cascades. Our specific aims are: 1) Identify and characterize candidate association and tetramerization domains in KCa channels. We will test the hypothesis that KCa channels contain specific protein domains that facilitate the tetramerization of some, and exclusion of other subunits. 2) Identify and characterize intermolecular KCa channel association domains and the resulting protein complexes. We will test the hypothesis that KCa channel a-subunits contain protein domains facilitating the intermolecular binding of other proteins to KCa channel tetramers resulting in novel Kca channel phenotypes. 3) Determine the role of alternative splicing of KCa channel a-subunits on protein complex formation. We will test the hypothesis that splice variants contain specific recognition domains for subsets of Kca channel binding proteins. 4) Determine the role of protein phosphorylation in modulating the identity and functionality of ion channel complexes. We will test the hypothesis that protein phosphorylation can dynamically rearrange the makeup of ion channel complexes, and hence alter the functionality of KCa channels within these complexes
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1 |