ArticleThe Journal of biological chemistry2009
NET37, a nuclear envelope transmembrane protein with glycosidase homology, is involved in myoblast differentiation.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 42 citations in OpenAlex.
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- The Pathology of Primary Familial Brain Calcification: Implications for Treatment.Neuroscience bulletin · 2023Review
- The primary familial brain calcification-associated protein MYORG is an α-galactosidase with restricted substrate specificity.PLoS biology · 2022Article
- Knockdown of myorg leads to brain calcification in zebrafish.Molecular brain · 2022Article
- Evolution and diversification of the nuclear envelope.Nucleus (Austin, Tex.) · 2021Article
- Mutation Analysis ofFrontiers in genetics · 2021Article
- Characterization of Glycoside Hydrolase Families 13 and 31 Reveals Expansion and Diversification of α-Amylase Genes in the PhlebotomineFrontiers in physiology · 2021Article
- A mutation map for human glycoside hydrolase genes.Glycobiology · 2020Article
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- MYORG Mutations: a Major Cause of Recessive Primary Familial Brain Calcification.Current neurology and neuroscience reports · 2019Review
- Article
- Messages from the voices within: regulation of signaling by proteins of the nuclear lamina.Current opinion in cell biology · 2018Review
- Spindle associated membrane protein 1 (Samp1) is required for the differentiation of muscle cells.Scientific reports · 2017Article
- Analysis of Nuclear Lamina Proteins in Myoblast Differentiation by Functional Complementation.Methods in molecular biology (Clifton, N.J.) · 2016Article
- Nonhuman genetics. Genomic basis for the convergent evolution of electric organs.Science (New York, N.Y.) · 2014Article
- The nuclear lamins: flexibility in function.Nature reviews. Molecular cell biology · 2013Review
- Outfits for different occasions: tissue-specific roles of Nuclear Envelope proteins.Current opinion in cell biology · 2012Review
- Deletion of muscle GRP94 impairs both muscle and body growth by inhibiting local IGF production.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2012Article
- A change in nuclear pore complex composition regulates cell differentiation.Developmental cell · 2012Article
- Nuclear lamina at the crossroads of the cytoplasm and nucleus.Journal of structural biology · 2012Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The nuclear lamina and its associated proteins are important for nuclear structure and chromatin organization and also have been implicated in the regulation of cell signaling and gene expression. In this study we demonstrate that the lamina-associated nuclear envelope transmembrane protein NET37 is required for myogenic differentiation of C2C12 cells. NET37, a member of glycosidase family 31, is highly expressed in mouse skeletal muscle and is strongly up-regulated during C2C12 differentiation. By protease mapping we show that its glycosidase homology domain is located in the lumen of the nuclear envelope/endoplasmic reticulum. When NET37 is depleted from proliferating myoblasts by RNAi, myogenic differentiation is significantly impaired, and there is a concomitant delay in up-regulation of the late myogenic transcription factor myogenin. We expressed silencing-resistant NET37 mutated at a conserved residue in the glycosidase domain and found that this predicted catalytically inactive protein is unable to support myogenesis in cells depleted of wild type NET37. Therefore, the enzymatic function of NET37 appears to be important for myogenic differentiation. C2C12 cells depleted of NET37 have reduced activation of Akt after shifting to differentiation medium and are defective in insulin like growth factor-II (IGF-II) secretion, an autocrine/paracrine factor involved in Akt activation. We also observed that pro-IGF-II co-immunoprecipitates with NET37. Based on our results, we propose that NET37 has a role in IGF-II maturation in the secretory pathway during myoblast differentiation. The localization of NET37 at the nuclear envelope raises the possibility that it may coordinate myogenic events between the nuclear interior and the endoplasmic reticulum lumen via transmembrane communication.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.