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Dane M. Chetkovich

Researcher at Vanderbilt University Medical Center

Publications -  23
Citations -  3042

Dane M. Chetkovich is an academic researcher from Vanderbilt University Medical Center. The author has contributed to research in topics: Postsynaptic potential & HCN channel. The author has an hindex of 9, co-authored 19 publications receiving 2786 citations. Previous affiliations of Dane M. Chetkovich include Vanderbilt University & University of California, San Francisco.

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Journal ArticleDOI

PSD-95 Involvement in Maturation of Excitatory Synapses

TL;DR: It is found that overexpression of PSD-95 in hippocampal neurons can drive maturation of glutamatergic synapses and this results demonstrate that PSd-95 can orchestrate synaptic development and are suggestive of roles for PSD -95 in synapse stabilization and plasticity.
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Stargazin regulates synaptic targeting of AMPA receptors by two distinct mechanisms

TL;DR: Stargazer, an ataxic and epileptic mutant mouse, lacks functional AMPA receptors on cerebellar granule cells, and expression of a mutant stargazin lacking the PDZ-binding domain in hippocampal pyramidal cells disrupts synaptic AMPA receptor receptors, indicating that st argazin-like mechanisms for targeting AM PA receptors may be widespread in the central nervous system.
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Dual Palmitoylation of Psd-95 Mediates Its Vesiculotubular Sorting, Postsynaptic Targeting, and Ion Channel Clustering

TL;DR: It is found that PSD-95 transiently associates with a perinuclear membranous compartment and traffics with vesiculotubular structures, which migrate in a microtubule-dependent manner, and in brain, it occurs not only at PSDs but also in association with intracellular smooth tubular structures in dendrites and spines.
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Phosphorylation of the Postsynaptic Density-95 (PSD-95)/Discs Large/Zona Occludens-1 Binding Site of Stargazin Regulates Binding to PSD-95 and Synaptic Targeting of AMPA Receptors

TL;DR: It is suggested that phosphorylation of the stargazin PDZ ligand can disrupt st argazin interaction with PSD-95 and thereby regulate synaptic AMPAR function.
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Postsynaptic Targeting of Alternative Postsynaptic Density-95 Isoforms by Distinct Mechanisms

TL;DR: Molecular and functional heterogeneity in synaptic PSD95 complexes are identified and critical roles for L27 domain interactions and Hrs regulated vesicular trafficking in postsynaptic protein clustering are revealed.