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Palmitoylation-dependent CDKL5-PSD-95 interaction regulates synaptic targeting of CDKL5 and dendritic spine development
scientific journal article
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scholarly article
1 reference
stated in
PubMed
PubMed ID
23671101
retrieved
21 March 2017
title
Palmitoylation-dependent CDKL5-PSD-95 interaction regulates synaptic targeting of CDKL5 and dendritic spine development
(English)
1 reference
stated in
PubMed
PubMed ID
23671101
retrieved
21 March 2017
main subject
dendritic spine
1 reference
based on heuristic
inferred from title
author name string
Yong-Chuan Zhu
series ordinal
1
1 reference
stated in
PubMed
PubMed ID
23671101
retrieved
21 March 2017
Dan Li
series ordinal
2
1 reference
stated in
PubMed
PubMed ID
23671101
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21 March 2017
Lu Wang
series ordinal
3
1 reference
stated in
PubMed
PubMed ID
23671101
retrieved
21 March 2017
Bin Lu
series ordinal
4
1 reference
stated in
PubMed
PubMed ID
23671101
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21 March 2017
Jing Zheng
series ordinal
5
1 reference
stated in
PubMed
PubMed ID
23671101
retrieved
21 March 2017
Shi-Lin Zhao
series ordinal
6
1 reference
stated in
PubMed
PubMed ID
23671101
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21 March 2017
Rong Zeng
series ordinal
7
1 reference
stated in
PubMed
PubMed ID
23671101
retrieved
21 March 2017
Zhi-Qi Xiong
series ordinal
8
1 reference
stated in
PubMed
PubMed ID
23671101
retrieved
21 March 2017
language of work or name
English
0 references
publication date
28 May 2013
1 reference
stated in
PubMed
PubMed ID
23671101
retrieved
21 March 2017
published in
Proceedings of the National Academy of Sciences of the United States of America
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stated in
PubMed
PubMed ID
23671101
retrieved
21 March 2017
volume
110
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PubMed
PubMed ID
23671101
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21 March 2017
issue
22
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PubMed
PubMed ID
23671101
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21 March 2017
page(s)
9118–9123
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PubMed
PubMed ID
23671101
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21 March 2017
cites work
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What we know and would like to know about CDKL5 and its involvement in epileptic encephalopathy
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CDKL5, a protein associated with rett syndrome, regulates neuronal morphogenesis via Rac1 signaling
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Mobile DHHC palmitoylating enzyme mediates activity-sensitive synaptic targeting of PSD-95
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23 March 2017
CDKL5 expression is modulated during neuronal development and its subcellular distribution is tightly regulated by the C-terminal tail
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Palmitoylation: policing protein stability and traffic
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Membrane-associated guanylate kinases regulate adhesion and plasticity at cell junctions
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CDKL5 belongs to the same molecular pathway of MeCP2 and it is responsible for the early-onset seizure variant of Rett syndrome
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Mutations in the X-linked cyclin-dependent kinase-like 5 (CDKL5/STK9) gene are associated with severe neurodevelopmental retardation
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23 March 2017
Direct interactions between PSD-95 and stargazin control synaptic AMPA receptor number
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23 March 2017
Identification and characterization of a novel serine-threonine kinase gene from the Xp22 region
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Binding of neuroligins to PSD-95
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Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alpha1-syntrophin mediated by PDZ domains
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Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95
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PSD-95 involvement in maturation of excitatory synapses
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Loss of CDKL5 disrupts kinome profile and event-related potentials leading to autistic-like phenotypes in mice.
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TrkB and protein kinase Mζ regulate synaptic localization of PSD-95 in developing cortex
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PSD-95-like membrane associated guanylate kinases (PSD-MAGUKs) and synaptic plasticity
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Protein palmitoylation in neuronal development and synaptic plasticity
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PubMed Central
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Dynamic protein palmitoylation in cellular signaling
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PSD-95 promotes synaptogenesis and multiinnervated spine formation through nitric oxide signaling.
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Synaptic trafficking of glutamate receptors by MAGUK scaffolding proteins
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3 June 2018
PSD-95 is required for activity-driven synapse stabilization
1 reference
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PubMed Central
reference URL
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3 June 2018
CDKL5/STK9 is mutated in Rett syndrome variant with infantile spasms
1 reference
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PubMed Central
reference URL
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3 June 2018
Protein palmitoylation: a regulator of neuronal development and function
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PubMed Central
reference URL
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3 June 2018
Dual palmitoylation of PSD-95 mediates its vesiculotubular sorting, postsynaptic targeting, and ion channel clustering
1 reference
stated in
PubMed Central
reference URL
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3 June 2018
Synaptic targeting of the postsynaptic density protein PSD-95 mediated by lipid and protein motifs
1 reference
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PubMed Central
reference URL
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3 June 2018
Reversible palmitoylation of signaling proteins
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3670390
retrieved
3 June 2018
CDKL5 ensures excitatory synapse stability by reinforcing NGL-1-PSD95 interaction in the postsynaptic compartment and is impaired in patient iPSC-derived neurons.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1073%2FPNAS.1300003110
retrieved
21 January 2018
CDKL5/Stk9 kinase inactivation is associated with neuronal developmental disorders.
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1073%2FPNAS.1300003110
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21 January 2018
N-terminal palmitoylation of PSD-95 regulates association with cell membranes and interaction with K+ channel Kv1.4.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1073%2FPNAS.1300003110
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21 January 2018
Synaptic strength regulated by palmitate cycling on PSD-95.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1073%2FPNAS.1300003110
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21 January 2018
Inhibition of protein palmitoylation, raft localization, and T cell signaling by 2-bromopalmitate and polyunsaturated fatty acids.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1073%2FPNAS.1300003110
retrieved
21 January 2018
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.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3670390
retrieved
26 November 2018
Heterogeneity in the molecular composition of excitatory postsynaptic sites during development of hippocampal neurons in culture.
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3670390
retrieved
26 November 2018
Identifiers
DOI
10.1073/PNAS.1300003110
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
704139
ADS bibcode
2013PNAS..110.9118Z
0 references
OpenCitations bibliographic resource ID
704139
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
704139
PMCID
3670390
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
704139
PubMed ID
23671101
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
704139
ResearchGate publication ID
236740940
0 references
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