A sex difference in the response of the rodent postsynaptic density to synGAP haploinsufficiency

SynGAP is a postsynaptic density (PSD) protein that binds to PDZ domains of the scaffold protein PSD-95. We previously reported that heterozygous deletion of in mice is correlated with increased steady-state levels of other key PSD proteins that bind PSD-95, although the level of PSD-95 remains cons...

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Published ineLife Vol. 9
Main Authors Mastro, Tara L, Preza, Anthony, Basu, Shinjini, Chattarji, Sumantra, Till, Sally M, Kind, Peter C, Kennedy, Mary B
Format Journal Article
LanguageEnglish
Published England eLife Science Publications, Ltd 15.01.2020
eLife Sciences Publications Ltd
eLife Sciences Publications, Ltd
Subjects
Animals
Biochemistry and Chemical Biology
CRISPR
CRISPR-Cas Systems
Datasets
Female
Females
Glutamate
glutamate receptor
Glutamic acid receptors
GTPase-Activating Proteins - genetics
GTPase-Activating Proteins - metabolism
Haploinsufficiency
Kinases
Male
Males
Mice
Mice, Knockout
Mutation
Neuroscience
Phosphorylation
Post-Synaptic Density - metabolism
Postsynaptic density
Postsynaptic density proteins
Protein binding
Proteins
Research Advance
Rodents
Scientific equipment industry
Sex Factors
synaptic plasticity
synGAP
α-Amino-3-hydroxy-5-methyl-4-isoxazole propionic acid
Canada
United States
mouse
chemical biology
rat
glutamate receptor
neuroscience
biochemistry
synGAP
synaptic plasticity
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Abstract SynGAP is a postsynaptic density (PSD) protein that binds to PDZ domains of the scaffold protein PSD-95. We previously reported that heterozygous deletion of in mice is correlated with increased steady-state levels of other key PSD proteins that bind PSD-95, although the level of PSD-95 remains constant (Walkup et al., 2016). For example, the ratio to PSD-95 of Transmembrane AMPA-Receptor-associated Proteins (TARPs), which mediate binding of AMPA-type glutamate receptors to PSD-95, was increased in young mice. Here we show that only females and not males show a highly significant correlation between an increase in TARP and a decrease in synGAP in the PSDs of rodents. The data reveal a sex difference in the adaptation of the PSD scaffold to synGAP haploinsufficiency.
AbstractList SynGAP is a postsynaptic density (PSD) protein that binds to PDZ domains of the scaffold protein PSD-95. We previously reported that heterozygous deletion of Syngap1 in mice is correlated with increased steady-state levels of other key PSD proteins that bind PSD-95, although the level of PSD-95 remains constant (Walkup et al., 2016). For example, the ratio to PSD-95 of Transmembrane AMPA-Receptor-associated Proteins (TARPs), which mediate binding of AMPA-type glutamate receptors to PSD-95, was increased in young Syngap1 +/- mice. Here we show that only females and not males show a highly significant correlation between an increase in TARP and a decrease in synGAP in the PSDs of Syngap1 +/- rodents. The data reveal a sex difference in the adaptation of the PSD scaffold to synGAP haploinsufficiency.
SynGAP is a postsynaptic density (PSD) protein that binds to PDZ domains of the scaffold protein PSD-95. We previously reported that heterozygous deletion of Syngap1 in mice is correlated with increased steady-state levels of other key PSD proteins that bind PSD-95, although the level of PSD-95 remains constant (Walkup et al., 2016). For example, the ratio to PSD-95 of Transmembrane AMPA-Receptor-associated Proteins (TARPs), which mediate binding of AMPA-type glutamate receptors to PSD-95, was increased in young Syngap1+/-mice. Here we show that only females and not males show a highly significant correlation between an increase in TARP and a decrease in synGAP in the PSDs of Syngap1+/-rodents. The data reveal a sex difference in the adaptation of the PSD scaffold to synGAP haploinsufficiency.
SynGAP is a postsynaptic density (PSD) protein that binds to PDZ domains of the scaffold protein PSD-95. We previously reported that heterozygous deletion of Syngap1 in mice is correlated with increased steady-state levels of other key PSD proteins that bind PSD-95, although the level of PSD-95 remains constant (Walkup et al., 2016). For example, the ratio to PSD-95 of Transmembrane AMPA-Receptor-associated Proteins (TARPs), which mediate binding of AMPA-type glutamate receptors to PSD-95, was increased in young Syngap1.sup.+/-mice. Here we show that only females and not males show a highly significant correlation between an increase in TARP and a decrease in synGAP in the PSDs of Syngap1.sup.+/-rodents. The data reveal a sex difference in the adaptation of the PSD scaffold to synGAP haploinsufficiency.
SynGAP is a postsynaptic density (PSD) protein that binds to PDZ domains of the scaffold protein PSD-95. We previously reported that heterozygous deletion of in mice is correlated with increased steady-state levels of other key PSD proteins that bind PSD-95, although the level of PSD-95 remains constant (Walkup et al., 2016). For example, the ratio to PSD-95 of Transmembrane AMPA-Receptor-associated Proteins (TARPs), which mediate binding of AMPA-type glutamate receptors to PSD-95, was increased in young mice. Here we show that only females and not males show a highly significant correlation between an increase in TARP and a decrease in synGAP in the PSDs of rodents. The data reveal a sex difference in the adaptation of the PSD scaffold to synGAP haploinsufficiency.
Audience Academic
Author Basu, Shinjini
Chattarji, Sumantra
Till, Sally M
Mastro, Tara L
Kennedy, Mary B
Kind, Peter C
Preza, Anthony
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/31939740$$D View this record in MEDLINE/PubMed
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Keywords mouse
chemical biology
rat
glutamate receptor
neuroscience
biochemistry
synGAP
synaptic plasticity
Language English
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Snippet SynGAP is a postsynaptic density (PSD) protein that binds to PDZ domains of the scaffold protein PSD-95. We previously reported that heterozygous deletion of...
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Aggregation Database
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SubjectTerms Animals
Biochemistry and Chemical Biology
CRISPR
CRISPR-Cas Systems
Datasets
Female
Females
Glutamate
glutamate receptor
Glutamic acid receptors
GTPase-Activating Proteins - genetics
GTPase-Activating Proteins - metabolism
Haploinsufficiency
Kinases
Male
Males
Mice
Mice, Knockout
Mutation
Neuroscience
Phosphorylation
Post-Synaptic Density - metabolism
Postsynaptic density
Postsynaptic density proteins
Protein binding
Proteins
Research Advance
Rodents
Scientific equipment industry
Sex Factors
synaptic plasticity
synGAP
α-Amino-3-hydroxy-5-methyl-4-isoxazole propionic acid
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Title A sex difference in the response of the rodent postsynaptic density to synGAP haploinsufficiency
URI https://www.ncbi.nlm.nih.gov/pubmed/31939740
https://www.proquest.com/docview/2368518278
https://search.proquest.com/docview/2338998684
https://pubmed.ncbi.nlm.nih.gov/PMC6994236
https://doaj.org/article/a09aac89c04d418884f82e7fb1029d4d
Volume 9
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