The mouse synemin gene encodes three intermediate filament proteins generated by alternative exon usage and different open reading frames

Xue, Zhigang; Chéraud, Yvonnick; Brocheriou, Valérie; Izmiryan, Araksya; Titeux, Matthias; Paulin, Denise; Li, Z

doi:10.1016/j.yexcr.2004.04.023

Cited by 54 publications

(72 citation statements)

References 32 publications

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“…-/-cells (Xue et al, 2004). Skeletal and cardiac muscle cells also co-express synemin and desmin, but not vimentin, further suggesting that vimentin is not required for synemin to incorporate into a desmin IF network.…”

Section: Desmentioning

confidence: 94%

“…Skeletal and cardiac muscle cells also co-express synemin and desmin, but not vimentin, further suggesting that vimentin is not required for synemin to incorporate into a desmin IF network. In these cells, the absence of desmin leads to greatly reduced synemin protein levels (Carlsson et al, 2000;Xue et al, 2004).…”

Section: Desmentioning

confidence: 99%

“…Genomic DNA contamination was avoided by treating samples with RNase-free DNase I. cDNA synthesis was performed with Thermoscript reverse transcriptase (Invitrogen) using an oligo(dT) 20 primer. RT-PCR of murine synemin isoforms was performed using the conditions and the P2 and P5 primers described by Xue et al (Xue et al, 2004). These primers amplify all synemin isoforms.…”

Section: Qualitative and Quantitative Pcrmentioning

confidence: 99%

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Synemin is expressed in reactive astrocytes in neurotrauma and interacts differentially with vimentin and GFAP intermediate filament networks

Jing

Wilhelmsson

Goodwill

et al. 2007

Journal of Cell Science

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GFAP IFs like an IF-associated protein rather than like a polymerization partner, whereas the opposite was true for synemin interaction with vimentin. In transfection experiments, synemin did not incorporate into normal, filamentous GFAP networks, but integrated into vimentin and GFAP heteropolymeric networks. Thus, alongside GFAP, vimentin and nestin, reactive astrocytes contain synemin, whose accumulation is suppressed posttranscriptionally in the absence of a polymerization partner. In astrocytes, this partner is vimentin and not GFAP, which implies a functional difference between these two type III IF proteins.

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Section: Desmentioning

confidence: 94%

Section: Desmentioning

confidence: 99%

Section: Qualitative and Quantitative Pcrmentioning

confidence: 99%

See 1 more Smart Citation

Synemin is expressed in reactive astrocytes in neurotrauma and interacts differentially with vimentin and GFAP intermediate filament networks

Jing

Wilhelmsson

Goodwill

et al. 2007

Journal of Cell Science

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“…First identified as a high-molecular-mass protein associated with desmin and vimentin filaments in muscle (Granger and Lazarides, 1980), synemin expression was later detected in different tissues and cell types, including the nervous system, endothelial cells, retinal cells and hepatic stellate cells (Hirako et al, 2003;Izmiryan et al, 2006;Izmiryan et al, 2009;Izmiryan et al, 2010;Schmitt-Graeff et al, 2006;Tawk et al, 2003;Uyama et al, 2006). Three synemin isoforms differing in their C-terminal tails -a-synemin (also known as synemin H, 180 kDa), b-synemin (also known as synemin M, 150 kDa) and synemin L (41 kDa) -are produced by alternative splicing and are differentially regulated during embryonic development (Titeux et al, 2001;Xue et al, 2004). b-synemin is expressed in pluripotent embryonic stem cells, whereas both a-and bsynemin are expressed in multipotent neural stem cells in the subventricular zone of the adult brain (de Souza Martins et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

“…Consequently, synemin filaments are unstable and delocalised in the cells of mice lacking desmin or vimentin (Carlsson et al, 2000;Izmiryan et al, 2006;Izmiryan et al, 2009;Jing et al, 2007;Xue et al, 2004). Synemin also interacts with a-actinin, plectin 1, zyxin, and three components of the dystrophin-associated protein complex, dystrophin, utrophin and a-dystrobrevin (Bellin et al, 1999;Bhosle et al, 2006;Hijikata et al, 2008;Mizuno et al, 2001;Sun et al, 2010a).…”

Section: Introductionmentioning

confidence: 99%

Synemin acts as a regulator of signalling molecules in skeletal muscle hypertrophy

Li¹,

Parlakian²,

Coletti³

et al. 2014

Journal of Cell Science

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Synemin, a type IV intermediate filament (IF) protein, forms a bridge between IFs and cellular membranes. As an A-kinase-anchoring protein, it also provides temporal and spatial targeting of protein kinase A (PKA). However, little is known about its functional roles in either process. To better understand its functions in muscle tissue, we generated synemin-deficient (Synm 2/2 ) mice. Synm 2/2 mice displayed normal development and fertility but showed a mild degeneration and regeneration phenotype in myofibres and defects in sarcolemma membranes. Following mechanical overload, Synm 2/2 mice muscles showed a higher hypertrophic capacity with increased maximal force and fatigue resistance compared with control mice. At the molecular level, increased remodelling capacity was accompanied by decreased myostatin (also known as GDF8) and atrogin (also known as FBXO32) expression, and increased follistatin expression. Furthermore, the activity of muscle-mass control molecules (the PKA RIIa subunit, p70S6K and CREB1) was increased in mutant mice. Finally, analysis of muscle satellite cell behaviour suggested that the absence of synemin could affect the balance between self-renewal and differentiation of these cells. Taken together, our results show that synemin is necessary to maintain membrane integrity and regulates signalling molecules during muscle hypertrophy.

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Different expression of synemin isoforms in glia and neurons during nervous system development

Izmiryan

Chéraud

Khanamiryan

et al. 2006

Glia

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The synemin gene encodes proteins belonging to the intermediate filament family. These proteins confer resistance to mechanical stress and modulate cell shape. Three synemin isoforms, of 180 (H), 150 (M) and 41 (L) kDa, are produced by alternative splicing of the pre-mRNA and are regulated differently during development. The three isoforms differ in their C-terminal tail domains, while their IF rod domains are identical. Synemins H/M occurred together with nestin and vimentin in glial progenitors during the early differentiation of the developing mouse central nervous system. They are later found in GFAP-labeled cells. In contrast, the L isoform appeared only in neurons, together with neurofilaments and betaIII-tubulin in the brain after birth. However, synemin L appeared from E13 in the peripheral nervous system, where it was confined to the neurons of spinal ganglia. In the meantime, the synemin H/M isoforms were found in both the neurons and Schwann cells of the sensorial ganglia from E11. Tissue fractionation and purification of IFs from adult mouse spinal cord revealed that the synemin L isoform binds to neurofilaments associated with the membrane compartment. This report describes the synthesis of the three synemin isoforms by selective cell types, and their temporal and spatial distributions. Mechanisms specific to neurons and glia probably control the splicing of the common synemin mRNA and the synthesis of each synemin isoform.

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The mouse synemin gene encodes three intermediate filament proteins generated by alternative exon usage and different open reading frames

Cited by 54 publications

References 32 publications

Synemin is expressed in reactive astrocytes in neurotrauma and interacts differentially with vimentin and GFAP intermediate filament networks

Synemin is expressed in reactive astrocytes in neurotrauma and interacts differentially with vimentin and GFAP intermediate filament networks

Synemin acts as a regulator of signalling molecules in skeletal muscle hypertrophy

Different expression of synemin isoforms in glia and neurons during nervous system development

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