Regulation of presynaptic cellular function

McGee, Richard

doi:10.1007/bf00225284

Cited by 6 publications

(3 citation statements)

References 50 publications

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“…We then evaluated the relationship between Malat1 and synapses. Neuro2a cells express genes related to synaptic function, but do not generate synapses per se (McGee, 1980; Spoerri et al , 1980). We, therefore, used well‐characterized primary hippocampal neuron cultures for examining the function of Malat1 in synapse formation or development.…”

Section: Resultsmentioning

confidence: 99%

A long nuclear-retained non-coding RNA regulates synaptogenesis by modulating gene expression

Bernard

Prasanth

Tripathi

et al. 2010

EMBO J

674

579

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A growing number of long nuclear-retained non-coding RNAs (ncRNAs) have recently been described. However, few functions have been elucidated for these ncRNAs. Here, we have characterized the function of one such ncRNA, identified as metastasis-associated lung adenocarcinoma transcript 1 (Malat1). Malat1 RNA is expressed in numerous tissues and is highly abundant in neurons. It is enriched in nuclear speckles only when RNA polymerase II-dependent transcription is active. Knock-down studies revealed that Malat1 modulates the recruitment of SR family pre-mRNA-splicing factors to the transcription site of a transgene array. DNA microarray analysis in Malat1-depleted neuroblastoma cells indicates that Malat1 controls the expression of genes involved not only in nuclear processes, but also in synapse function. In cultured hippocampal neurons, knock-down of Malat1 decreases synaptic density, whereas its over-expression results in a cellautonomous increase in synaptic density. Our results suggest that Malat1 regulates synapse formation by modulating the expression of genes involved in synapse formation and/or maintenance.

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Section: Resultsmentioning

confidence: 99%

A long nuclear-retained non-coding RNA regulates synaptogenesis by modulating gene expression

Bernard

Prasanth

Tripathi

et al. 2010

EMBO J

674

579

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“…The PC12 cells, derived from pheochromocytoma of the rat adrenal medulla, were generously provided by Dr. Lung-Sen Kao [18], [19]. The cells were cultured in DMEM containing 10% horse serum and 5% fetal bovine serum, and were then incubated at 37°C in an atmosphere containing 10% CO 2 .…”

Section: Methodsmentioning

confidence: 99%

Changes in Plasma Membrane Surface Potential of PC12 Cells as Measured by Kelvin Probe Force Microscopy

et al. 2012

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The plasma membrane of a cell not only works as a physical barrier but also mediates the signal relay between the extracellular milieu and the cell interior. Various stimulants may cause the redistribution of molecules, like lipids, proteins, and polysaccharides, on the plasma membrane and change the surface potential (Φ s ). In this study, the Φ s s of PC12 cell plasma membranes were measured by atomic force microscopy in Kelvin probe mode (KPFM). The skewness values of the Φ s s distribution histogram were found to be mostly negative, and the incorporation of negatively charged phosphatidylserine shifted the average skewness values to positive. After being treated with H 2 O 2 , dopamine, or Zn 2+ , phosphatidylserine was found to be translocated to the membrane outer leaflet and the averaged skewness values were changed to positive values. These results demonstrated that KPFM can be used to monitor cell physiology status in response to various stimulants with high spatial resolution.

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“…The expression of RGS9-2, G␤5, and R7BP in vivo is restricted to neuronal tissues, which suggests that much of their native properties may be dependent upon the specific intracellular environment of neurons. Therefore, we chose to use the NG108-15 mouse neuroblastoma/rat glioma hybrid cells, which share many common properties with native differentiated neurons (29).…”

Section: R7bp Targets Rgs9-2 Localization To the Plasma Membrane-wementioning

confidence: 99%

Subcellular Targeting of RGS9-2 Is Controlled by Multiple Molecular Determinants on Its Membrane Anchor, R7BP

Song

Waataja

Martemyanov

2006

Journal of Biological Chemistry

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RGS9-2, a member of the R7 regulators of G protein signaling (RGS) protein family of neuronal RGS, is a critical regulator of G protein signaling. In striatal neurons, RGS9-2 is tightly associated with a novel palmitoylated protein, R7BP (R7 family binding protein). Here we report that R7BP acts to target the localization of RGS9-2 to the plasma membrane. Examination of the subcellular distribution in native striatal neurons revealed that both R7BP and RGS9-2 are almost entirely associated with the neuronal membranes. In addition to the plasma membrane, a large portion of RGS9-2 was found in the neuronal specializations, the postsynaptic densities, where it forms complexes with R7BP and its constitutive partner G␤5. Using site-directed mutagenesis we found that the molecular determinants that specify the subcellular targeting of RGS9-2⅐G␤5⅐R7BP complex are contained within the 21 C-terminal amino acids of R7BP. This function of the C terminus was found to require the synergistic contributions of its two distinct elements, a polybasic motif and palmitoylated cysteines, which when combined are sufficient for directing the intracellular localization of the constituent protein. In differentiated neurons, the C-terminal targeting motif of R7BP was found to be essential for mediating its postsynaptic localization. In addition to the plasma membrane targeting elements, we identified two functional nuclear localization sequences that can mediate the import of R7BP into the nucleus upon depalmitoylation. These findings provide a mechanism for the subcellular targeting of RGS9-2 in neurons.G protein signaling pathways mediate a wide range of critical neuronal processes (1). The normal functioning of these pathways is dependent on the tight control of signal duration mediated by regulators of G protein signaling (RGS) 2 proteins (2, 3). RGS proteins act to control the inactivation of heterotrimeric G proteins by dramatically accelerating the rate of their GTP hydrolysis (4, 5). Much recent attention has been focused on the R7 subfamily of RGS proteins due to their emerging roles in the regulation of a variety of critical neuronal functions (6, 7). The R7 subfamily contains four highly homologous proteins, RGS6, RGS7, RGS9, and RGS11, which are expressed exclusively in the nervous system (8) as constitutive complexes with a type 5 G protein ␤ subunit (G␤5) (9 -11).RGS9, with its two splice isoforms, is one of the best-studied members of the R7 subfamily. The short isoform RGS9-1 is expressed in the photoreceptor neurons where it regulates the visual signal transduction cascade (12, 13). The long splice isoform RGS9-2 is predominantly expressed in the striatum and the central nervous system structures, mediating nociceptive responses where it was shown to regulate dopamine and -opioid pathways (14 -17). Disruption of RGS9-2 in mice resulted in the stimulation of locomotor and reward behavior, increased physical dependence and analgesic effects of morphine, and movement disorders (15)(16)(17). In photoreceptors, the function ...

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Regulation of presynaptic cellular function

Cited by 6 publications

References 50 publications

A long nuclear-retained non-coding RNA regulates synaptogenesis by modulating gene expression

A long nuclear-retained non-coding RNA regulates synaptogenesis by modulating gene expression

Changes in Plasma Membrane Surface Potential of PC12 Cells as Measured by Kelvin Probe Force Microscopy

Subcellular Targeting of RGS9-2 Is Controlled by Multiple Molecular Determinants on Its Membrane Anchor, R7BP

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