E14.5-born neurons at P3 repress L4 neuron-type and induce L2/3 neuron-type genes upon Kir2.1 in utero electroporation
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ABSTRACT:
ORGANISM(S): Mus musculus
PROVIDER: GSE115627 | GEO | 2018/06/12
REPOSITORIES: GEO
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Project description:E14.5-born neurons at P3 repress L4 neuron-type and induce L2/3 neuron-type genes upon Kir2.1 in utero electroporation
| PRJNA475586 | ENA
Project description:Experimental in vivo hyperpolarization of E14.5 apical progenitors shifted their transcriptional programs with precocious generation of intermediate progenitors, and a forward shift in the laminar, molecular, morphological and circuit features of their neuronal progeny. In particular, we reported an overall repression of L4-type neuronal genes and a premature induction of L2/3-type neuronal genes following Kir2.1 overexpression.
2018-06-12 | GSE115628 | GEO
Project description:Kir2.1, an inward rectifier potassium channel, plays an important role in controlling membrane potential specially in cardiomyocytes. Here we explore its interactome via proximity biotin labeling and affinity purification approach (BioID). First, BioID membrane controls were generated with randomly selected transmembrane domains from yeast proteins, demonstrating the identification of membrane-associated proteins more than GFP or NLS controls. Using this control and a mutation from Andersen-Tawil syndrome which causes Kir2.1 Golgi accumulation, we have identified the most comprehensive Kir2.1 interactome and also found clues to its spatial information in subcellular levels. The interactome is showing that Kir2.1 in plasma membrane is surrounded by desmosome, integrin, cadherin and dystrophin-glycoprotein complex complexes, and supported by MAGUK family scaffold proteins. On the other hand, Kir2.1 mutant BioID revealed the COPII-mediated delivery of Kir2.1 from ER to Golgi and lysosome-mediated degradation of Golgi-accumulated and/or retrograde Kir2.1. Validating the interactome with co-immunoprecipitation, confocal microscope, and patch clamp analysis, we concluded that Kir2.1 is located in the defined membrane environment and is actively regulated by endosomal sorting for lysosome degradation.
2020-06-17 | PXD011004 | Pride
Project description:Misfolded membrane proteins are retained in the endoplasmic reticulum (ER) and are subject to the ER associated degradation pathway, which clears the secretory pathway of potentially toxic species. While the transcriptional response to environmental stressors has been extensively studied, limited data exist describing the cellular response to misfolded membrane proteins. To this end, we expressed and then compared the transcriptional profiles elicited by the synthesis of three ER retained, misfolded ion channels: The α subunit of the epithelial sodium channel, ENaC, the cystic fibrosis transmembrane conductance regulator, CFTR, and an inwardly rectifying potassium channel, Kir2.1, which vary in their mass, membrane topologies, and quaternary structures. To examine transcriptional profiles in a null background, the proteins were expressed in yeast, which was previously used to examine the degradation requirements for each substrate. Surprisingly, the proteins failed to induce a canonical unfolded protein response or heat shock response, although messages encoding several cytosolic and ER lumenal protein folding factors rose when αENaC or CFTR were expressed. In contrast, the levels of these genes were unaltered by Kir2.1 expression; instead, the yeast iron regulon was activated. Nevertheless, a significant number of genes that respond to various environmental stressors were upregulated by all three substrates, and when compared to previous microarray data we deduced the existence of a group of genes that reflect a novel misfolded membrane protein response. These data indicate that aberrant proteins in the ER elicit profound yet unique cellular responses. Yeast heterologously expressing αENaC, CFTR, Kir2.1 or harboring a vector control were grown under identical conditions (at least 3 biological replicates) and subject to gene expression analysis.
2014-09-10 | E-GEOD-61245 | biostudies-arrayexpress
Project description:Mitral cells in the mouse olfactory bulb are known to remodel their primary dendrites and form lateral dendrites during postnatal development. These processes are suppressed when neuronal activity is silenced by overexpression of Kir2.1 in mitral cells, indicating that neuronal activity in mitral cells is required. However, it is unclear what changes in gene expression lead to the remodeling of mitral cell dendrites in an activity-dependent manner. To address this, we performed a microarray-based analysis of gene expression in mitral cells during normal development and under the activity-silenced condition.
2021-04-13 | GSE171875 | GEO
Project description:Misfolded membrane proteins are retained in the endoplasmic reticulum (ER) and are subject to the ER associated degradation pathway, which clears the secretory pathway of potentially toxic species. While the transcriptional response to environmental stressors has been extensively studied, limited data exist describing the cellular response to misfolded membrane proteins. To this end, we expressed and then compared the transcriptional profiles elicited by the synthesis of three ER retained, misfolded ion channels: The α subunit of the epithelial sodium channel, ENaC, the cystic fibrosis transmembrane conductance regulator, CFTR, and an inwardly rectifying potassium channel, Kir2.1, which vary in their mass, membrane topologies, and quaternary structures. To examine transcriptional profiles in a null background, the proteins were expressed in yeast, which was previously used to examine the degradation requirements for each substrate. Surprisingly, the proteins failed to induce a canonical unfolded protein response or heat shock response, although messages encoding several cytosolic and ER lumenal protein folding factors rose when αENaC or CFTR were expressed. In contrast, the levels of these genes were unaltered by Kir2.1 expression; instead, the yeast iron regulon was activated. Nevertheless, a significant number of genes that respond to various environmental stressors were upregulated by all three substrates, and when compared to previous microarray data we deduced the existence of a group of genes that reflect a novel misfolded membrane protein response. These data indicate that aberrant proteins in the ER elicit profound yet unique cellular responses.
2014-09-10 | GSE61245 | GEO
Project description:Purpose:Mouse BMDM is the universal cell type of studying innate immunity.This study was to analyze LPS induced innate immune response and the relationship between the inward rectifier potassium channel Kir2.1 and LPS induced innate immune respone Methods: WT and Kcnj2 KO BMDM cells were treated with or without LPS for 6 hours in the presence of kir2.1 inhibitor ML133 or not. Then mRNA profiles of these samles were generated by High-throughput sequencing analysis, in triplicate, using illumina HiSeq 2000. And the differential mRNA profiles were analyzed. Results: mRNA profiles of more than 20000 genes were analyzed, and differential expression profiles were compared . Conclusions: Our study represents the first detailed analysis of transcriptomes of WT and Kcnj2 KO mouse BMDM treated with LPS or kir2.1 inhibitor, with biologic replicates, generated by RNA-seq technology. This data was useful to analyze the relationship between Kir2.1 and LPS induced innate immune respone
2022-04-05 | GSE146158 | GEO
Project description:Misfolded membrane proteins are retained in the endoplasmic reticulum (ER) and are subject to the ER associated degradation pathway, which clears the secretory pathway of potentially toxic species. While the transcriptional response to environmental stressors has been extensively studied, limited data exist describing the cellular response to misfolded membrane proteins. To this end, we expressed and then compared the transcriptional profiles elicited by the synthesis of three ER retained, misfolded ion channels: The α subunit of the epithelial sodium channel, ENaC, the cystic fibrosis transmembrane conductance regulator, CFTR, and an inwardly rectifying potassium channel, Kir2.1, which vary in their mass, membrane topologies, and quaternary structures. To examine transcriptional profiles in a null background, the proteins were expressed in yeast, which was previously used to examine the degradation requirements for each substrate. Surprisingly, the proteins failed to induce a canonical unfolded protein response or heat shock response, although messages encoding several cytosolic and ER lumenal protein folding factors rose when αENaC or CFTR were expressed. In contrast, the levels of these genes were unaltered by Kir2.1 expression; instead, the yeast iron regulon was activated. Nevertheless, a significant number of genes that respond to various environmental stressors were upregulated by all three substrates, and when compared to previous microarray data we deduced the existence of a group of genes that reflect a novel misfolded membrane protein response. These data indicate that aberrant proteins in the ER elicit profound yet unique cellular responses. Yeast heterologously expressing αENaC, CFTR, Kir2.1 or harboring a vector control were grown under identical conditions (at least 3 biological replicates) and subject to gene expression analysis.
2014-09-10 | E-GEOD-61244 | biostudies-arrayexpress
Project description:Misfolded membrane proteins are retained in the endoplasmic reticulum (ER) and are subject to the ER associated degradation pathway, which clears the secretory pathway of potentially toxic species. While the transcriptional response to environmental stressors has been extensively studied, limited data exist describing the cellular response to misfolded membrane proteins. To this end, we expressed and then compared the transcriptional profiles elicited by the synthesis of three ER retained, misfolded ion channels: The α subunit of the epithelial sodium channel, ENaC, the cystic fibrosis transmembrane conductance regulator, CFTR, and an inwardly rectifying potassium channel, Kir2.1, which vary in their mass, membrane topologies, and quaternary structures. To examine transcriptional profiles in a null background, the proteins were expressed in yeast, which was previously used to examine the degradation requirements for each substrate. Surprisingly, the proteins failed to induce a canonical unfolded protein response or heat shock response, although messages encoding several cytosolic and ER lumenal protein folding factors rose when αENaC or CFTR were expressed. In contrast, the levels of these genes were unaltered by Kir2.1 expression; instead, the yeast iron regulon was activated. Nevertheless, a significant number of genes that respond to various environmental stressors were upregulated by all three substrates, and when compared to previous microarray data we deduced the existence of a group of genes that reflect a novel misfolded membrane protein response. These data indicate that aberrant proteins in the ER elicit profound yet unique cellular responses. Yeast heterologously expressing αENaC, CFTR, Kir2.1 or harboring a vector control were grown under identical conditions (at least 3 biological replicates) and subject to gene expression analysis.
2014-09-10 | E-GEOD-61243 | biostudies-arrayexpress
Project description:Misfolded membrane proteins are retained in the endoplasmic reticulum (ER) and are subject to the ER associated degradation pathway, which clears the secretory pathway of potentially toxic species. While the transcriptional response to environmental stressors has been extensively studied, limited data exist describing the cellular response to misfolded membrane proteins. To this end, we expressed and then compared the transcriptional profiles elicited by the synthesis of three ER retained, misfolded ion channels: The α subunit of the epithelial sodium channel, ENaC, the cystic fibrosis transmembrane conductance regulator, CFTR, and an inwardly rectifying potassium channel, Kir2.1, which vary in their mass, membrane topologies, and quaternary structures. To examine transcriptional profiles in a null background, the proteins were expressed in yeast, which was previously used to examine the degradation requirements for each substrate. Surprisingly, the proteins failed to induce a canonical unfolded protein response or heat shock response, although messages encoding several cytosolic and ER lumenal protein folding factors rose when αENaC or CFTR were expressed. In contrast, the levels of these genes were unaltered by Kir2.1 expression; instead, the yeast iron regulon was activated. Nevertheless, a significant number of genes that respond to various environmental stressors were upregulated by all three substrates, and when compared to previous microarray data we deduced the existence of a group of genes that reflect a novel misfolded membrane protein response. These data indicate that aberrant proteins in the ER elicit profound yet unique cellular responses.
2014-09-10 | GSE61244 | GEO