Loss of Emerin Alters Myogenic Signaling and miRNA Expression in Mouse Myogenic Progenitors

Koch, Adam J.; Holaska, James M.

doi:10.1371/journal.pone.0037262

Cited by 29 publications

(66 citation statements)

References 60 publications

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“…Wildtype and emerin-null H2K mouse myogenic progenitors were a generous gift from Tatiana Cohen and Terry Partridge (Children’s National Medical Center, Washington, DC) and were isolated as previously described (Koch and Holaska 2012). Proliferating myogenic progenitors were grown in proliferative media consisting of complete high-glucose DMEM vitrogen) supplemented with 20 % heat-inactivated FBS (Invitrogen), 2 % chick embryo extract (Accurate Chemical), 2 % l -glutamine (Invitrogen), 1 % penicillin–streptomycin (Invitrogen) and 20 units/ml γ-interferon (Millipore).…”

Section: Methodsmentioning

confidence: 99%

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Emerin and histone deacetylase 3 (HDAC3) cooperatively regulate expression and nuclear positions of MyoD, Myf5, and Pax7 genes during myogenesis

2013

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The spatial organization of chromatin is critical in establishing cell-type dependent gene expression programs. The inner nuclear membrane protein emerin has been implicated in regulating global chromatin architecture. We show emerin associates with genomic loci of muscle differentiation promoting factors in murine myogenic progenitors, including Myf5 and MyoD. Prior to their transcriptional activation Myf5 and MyoD loci localized to the nuclear lamina in proliferating progenitors and moved to the nucleoplasm upon transcriptional activation during differentiation. The Pax7 locus, which is transcribed in proliferating progenitors, localized to the nucleoplasm and Pax7 moved to the nuclear lamina upon repression during differentiation. Localization of Myf5, MyoD, and Pax7 to the nuclear lamina and proper temporal expression of these genes required emerin and HDAC3. Interestingly, activation of HDAC3 catalytic activity rescued both Myf5 localization to the nuclear lamina and its expression. Collectively, these data support a model whereby emerin facilitates repressive chromatin formation at the nuclear lamina by activating the catalytic activity of HDAC3 to regulate the coordinated spatiotemporal expression of myogenic differentiation genes.

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Section: Methodsmentioning

confidence: 99%

“…Emerin-downregulated myoblasts also exhibit impaired differentiation (Frock et al 2006; Huber et al 2009). Further, signaling pathways important for skeletal muscle regeneration were disrupted in emerin-null myogenic progenitors, including Wnt, IGF-1, TGF-β, and Notch (Koch and Holaska 2012). …”

Section: Introductionmentioning

confidence: 99%

Emerin and histone deacetylase 3 (HDAC3) cooperatively regulate expression and nuclear positions of MyoD, Myf5, and Pax7 genes during myogenesis

2013

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“…Multiple LEM-D proteins directly interact with signaling effectors [9, 55, 56]. For example, emerin directly binds and regulates the flux of β-catenin into the nucleus (Figure 3A, [57]).…”

Section: Lem-d Proteins Regulate Transcription Factor Functionmentioning

confidence: 99%

“…For example, emerin directly binds and regulates the flux of β-catenin into the nucleus (Figure 3A, [57]). In the absence of emerin, levels of nuclear β-catenin increase, resulting in up-regulation of target genes [55, 57]. Similarly, emerin regulates nuclear envelope localization of other transcription factors, including LIM Domain Only 7 (Lmo7), a transcriptional activator involved in myogenic differentiation [58].…”

Section: Lem-d Proteins Regulate Transcription Factor Functionmentioning

confidence: 99%

Networking in the nucleus: a spotlight on LEM-domain proteins

Barton

Soshnev

Geyer

2015

Current Opinion in Cell Biology

168

151

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Proteins resident in the inner nuclear membrane and underlying nuclear lamina form a network that regulates nuclear functions. This review highlights a prominent family of nuclear lamina proteins that carries the LAP2-emerin-MAN1-domain (LEM-D). LEM-D proteins share an ability to bind lamins and tether repressive chromatin at the nuclear periphery. The importance of this family is underscored by findings that loss of individual LEM-D proteins causes progressive, tissue-restricted diseases, known as laminopathies. Diverse functions of LEM-D proteins are linked to interactions with unique and overlapping partners including signal transduction effectors, transcription factors and architectural proteins. Recent investigations suggest that LEM-D proteins form hubs within the nuclear lamina that integrate external signals important for tissue homeostasis and maintenance of progenitor cell populations.

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“…Koch and Holaska (2012) studied miRNA expression in X‐linked Emery–Dreifuss muscular dystrophy, which is caused by mutations in emerin ( EMD ). They performed miRNA expression profiling on emerin‐null mouse myogenic progenitor cells compared to wild‐type controls.…”

Section: Mirnas In Hereditary Laminopathiesmentioning

confidence: 99%

MicroRNAs in hereditary and sporadic premature aging syndromes and other laminopathies

et al. 2018

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SummaryHereditary and sporadic laminopathies are caused by mutations in genes encoding lamins, their partners, or the metalloprotease ZMPSTE24/FACE1. Depending on the clinical phenotype, they are classified as tissue‐specific or systemic diseases. The latter mostly manifest with several accelerated aging features, as in Hutchinson–Gilford progeria syndrome (HGPS) and other progeroid syndromes. MicroRNAs are small noncoding RNAs described as powerful regulators of gene expression, mainly by degrading target mRNAs or by inhibiting their translation. In recent years, the role of these small RNAs has become an object of study in laminopathies using in vitro or in vivo murine models as well as cells/tissues of patients. To date, few miRNAs have been reported to exert protective effects in laminopathies, including miR‐9, which prevents progerin accumulation in HGPS neurons. The recent literature has described the potential implication of several other miRNAs in the pathophysiology of laminopathies, mostly by exerting deleterious effects. This review provides an overview of the current knowledge of the functional relevance and molecular insights of miRNAs in laminopathies. Furthermore, we discuss how these discoveries could help to better understand these diseases at the molecular level and could pave the way toward identifying new potential therapeutic targets and strategies based on miRNA modulation.

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Loss of Emerin Alters Myogenic Signaling and miRNA Expression in Mouse Myogenic Progenitors

Cited by 29 publications

References 60 publications

Emerin and histone deacetylase 3 (HDAC3) cooperatively regulate expression and nuclear positions of MyoD, Myf5, and Pax7 genes during myogenesis

Emerin and histone deacetylase 3 (HDAC3) cooperatively regulate expression and nuclear positions of MyoD, Myf5, and Pax7 genes during myogenesis

Networking in the nucleus: a spotlight on LEM-domain proteins

MicroRNAs in hereditary and sporadic premature aging syndromes and other laminopathies

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