A novel nuclear structure containing the survival of motor neurons protein.

Liu, Q; Dreyfuss, Gideon

doi:10.1002/j.1460-2075.1996.tb00725.x

Cited by 695 publications

(676 citation statements)

References 58 publications

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“…3b,e). As originally shown in a HeLa (PV) subline (Liu and Dreyfuss 1996), the gems in UR61 cells were completely devoid of detectable Sm proteins or other spliceosomal components (Fig. 3i and data not shown).…”

Section: Differentiation Induces Accumulation Of Smn In Cajal Bodiessupporting

confidence: 78%

“…After several washes, cells were mounted in Vectashield medium (Vector Laboratories). Primary antibodies used were anti-coilin 204.10 rabbit serum (Bohmann et al 1995), anti-SMN monoclonal antibody (mAb) (Transduction Laboratories), anti-SMN 2B1 mAb (Liu and Dreyfuss 1996), anti-Gemin2/SIP1 E17 mAb (Liu et al 1997), anti-Sm C45 human serum, anti-U2B" 4G3 mAb, and anti-Nopp 140 rabbit serum RF12 (Meier and Blobel 1992). Cell samples were examined using a Zeiss 63× NA 1.4 PlanApo objective.…”

Section: Fluorescence Microscopy and Immunostainingmentioning

confidence: 99%

“…Since their discovery in 1996, gems have been identified only at the level of the light microscope (Liu and Dreyfuss 1996) and thus their ultrastructural identification has remained elusive. We took advantage of the abundance of gems in differentiated UR61 cells to characterize their structure by immunogold electron microscopy.…”

Section: Ultrastructural Characterization Of Gemsmentioning

confidence: 99%

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Targeting SMN to Cajal bodies and nuclear gems during neuritogenesis

et al. 2004

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Neurite outgrowth is a central feature of neuronal differentiation. PC12 cells are a good model system for studying the peripheral nervous system and the outgrowth of neurites. In addition to the dramatic changes observed in the cytoplasm, neuronal differentiation is also accompanied by striking changes in nuclear morphology. The large and sustained increase in nuclear transcription during neuronal differentiation requires synthesis of a large number of factors involved in pre-mRNA processing. We show that the number and composition of the nuclear subdomains called Cajal bodies and gems changes during the course of N-ras-induced neuritogenesis in the PC12-derived cell line UR61. The Cajal bodies found in undifferentiated cells are largely devoid of the survival of motor neurons (SMN) protein product. As cells shift to a differentiated state, SMN is not only globally upregulated, but is progressively recruited to Cajal bodies. Additional SMN foci (also known as Gemini bodies, gems) can also be detected. Using dual-immunogold labeling electron microscopy and mouse embryonic fibroblasts lacking the coilin protein, we show that gems clearly represent a distinct category of nuclear body.

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Section: Differentiation Induces Accumulation Of Smn In Cajal Bodiessupporting

confidence: 78%

Section: Fluorescence Microscopy and Immunostainingmentioning

confidence: 99%

Section: Ultrastructural Characterization Of Gemsmentioning

confidence: 99%

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Targeting SMN to Cajal bodies and nuclear gems during neuritogenesis

et al. 2004

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“…Once all baseline samples were collected, SMN protein was measured at PharmOptima (Portage, MI) using the company's proprietary electrochemiluminescence immunoassay based on the Meso Scale Discovery technology. The assay is a quantitative sandwich immunoassay, where a mouse monoclonal antibody (2B130) functions as the capture antibody and a rabbit polyclonal anti‐SMN antibody (Protein Tech, Cat. No.…”

Section: Methodsmentioning

confidence: 99%

Baseline results of the NeuroNEXT spinal muscular atrophy infant biomarker study

Kolb

Coffey

Yankey

et al. 2016

Ann Clin Transl Neurol

107

128

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ObjectiveThis study prospectively assessed putative promising biomarkers for use in assessing infants with spinal muscular atrophy (SMA).MethodsThis prospective, multi‐center natural history study targeted the enrollment of SMA infants and healthy control infants less than 6 months of age. Recruitment occurred at 14 centers within the NINDS National Network for Excellence in Neuroscience Clinical Trials (NeuroNEXT) Network. Infant motor function scales and putative electrophysiological, protein and molecular biomarkers were assessed at baseline and subsequent visits.ResultsEnrollment began November, 2012 and ended September, 2014 with 26 SMA infants and 27 healthy infants enrolled. Baseline demographic characteristics of the SMA and control infant cohorts aligned well. Motor function as assessed by the Test for Infant Motor Performance Items (TIMPSI) and the Children's Hospital of Philadelphia Infant Test of Neuromuscular Disorders (CHOP‐INTEND) revealed significant differences between the SMA and control infants at baseline. Ulnar compound muscle action potential amplitude (CMAP) in SMA infants (1.4 ± 2.2 mV) was significantly reduced compared to controls (5.5 ± 2.0 mV). Electrical impedance myography (EIM) high‐frequency reactance slope (Ohms/MHz) was significantly higher in SMA infants than controls SMA infants had lower survival motor neuron (SMN) mRNA levels in blood than controls, and several serum protein analytes were altered between cohorts.InterpretationBy the time infants were recruited and presented for the baseline visit, SMA infants had reduced motor function compared to controls. Ulnar CMAP, EIM, blood SMN mRNA levels, and serum protein analytes were able to distinguish between cohorts at the enrollment visit.

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“…Since the CBs that are devoid of SMN maintain high concentrations of snRNPs (Liu and Dreyfuss 1996;Hebert et al 2002), SMN is unlikely to be this factor. Previously, we showed that the C-terminal 214 amino acid (aa) residues of coilin are sufficient for interaction with SmB′, making coilin a candidate (Hebert et al 2001).…”

Section: Coilin Binds To the Sm-fold Regions Of Sm And Sm-like Proteinsmentioning

confidence: 99%

The C-terminal domain of coilin interacts with Sm proteins and U snRNPs

Pillai

Azzouz

et al. 2005

Chromosoma

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Coilin is the signature protein of the Cajal body (CB), a nuclear suborganelle involved in the biogenesis of small nuclear ribonucleoproteins (snRNPs). Newly imported Sm-class snRNPs are thought to traffic through CBs before proceeding to their final nuclear destinations. Loss of coilin function in mice leads to significant viability and fertility problems. Coilin interacts directly with the spinal muscular atrophy (SMA) protein via dimethylarginine residues in its C-terminal domain. Although coilin hypomethylation results in delocalization of survival of motor neurons (SMN) from CBs, high concentrations of snRNPs remain within these structures. Thus, CBs appear to be involved in snRNP maturation, but factors that tether snRNPs to CBs have not been described. In this report, we demonstrate that the coilin C-terminal domain binds directly to various Sm and Lsm proteins via their Sm motifs. We show that the region of coilin responsible for this binding activity is separable from that which binds to SMN. Interestingly, U2, U4, U5, and U6 snRNPs interact with the coilin C-terminal domain in a glutathione S-transferase (GST)-pulldown assay, whereas U1 and U7 snRNPs do not. Thus, the ability to interact with free Sm (and Lsm) proteins as well as with intact snRNPs, indicates that coilin and CBs may facilitate the modification of newly formed snRNPs, the regeneration of 'mature' snRNPs, or the reclamation of unassembled snRNP components.

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A novel nuclear structure containing the survival of motor neurons protein.

Cited by 695 publications

References 58 publications

Targeting SMN to Cajal bodies and nuclear gems during neuritogenesis

Targeting SMN to Cajal bodies and nuclear gems during neuritogenesis

Baseline results of the NeuroNEXT spinal muscular atrophy infant biomarker study

The C-terminal domain of coilin interacts with Sm proteins and U snRNPs

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