Biochemical and Biophysical Research Communications
Association of emerin with nuclear and cytoplasmic actin is regulated in differentiating myoblasts
Section snippets
Materials and methods
Cell culture and differentiation. C2C12 mouse myoblasts were grown in DMEM supplemented with 10% fetal calf serum. Myoblast cultures approaching confluence were shifted in differentiation medium (DMEM plus 1% fetal calf serum) and allowed to differentiate for the specified time points [16].
Transfection of cycling C2C12 myoblasts. A pEGFP-actin vector coding for cytoplasmic β actin was purchased from Clontech. Exponentially growing C2C12 myoblasts were transfected by using the FuGene
Results and discussion
We previously demonstrated that emerin is highly expressed in differentiated mouse and human myotubes and that both nuclear and cytoskeleton localization of emerin can be observed in these cells [15]. Emerin has been reported to interact with actin in C2C12 mouse myoblasts and to bind α actin in in vitro blot overlay assay [23]. The study here reported was aimed at the evaluation of emerin–actin interaction in differentiating muscle cells. To this purpose, emerin was immunoprecipitated from
Acknowledgements
The authors thank P. Sabatelli and I. Mura for the technical assistance. This work was supported by grants: E.C. project Myo-Cluster, Contract No. QLG1-1999-00870; P.F. 83/2001 “Ministero della Salute,” Italy; Fondazione Carisbo P.B. “Diagnosi, ricerca e trattamento nelle distrofie muscolari,” Italy.
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Lamin A involvement in ageing processes
2020, Ageing Research ReviewsCitation Excerpt :The ability to form complexes containing lamin A/C and its partners involved in mechanosignaling is heavily threatened in progeroid nuclei, a condition that in turn affects mechanosignaling (Capanni et al., 2009; Wu et al., 2014). Emerin is a main lamin A/C-binding partner at the nuclear membrane and interacts with actin and actin-associated proteins, i.e. it participates in the constitution of the nuclear peripheral functional network (Holaska et al., 2004; Lattanzi et al., 2003). The LINC complex is also severely affected in HGPS cells.
An actin-based nucleoskeleton involved in gene regulation and genome organization
2018, Biochemical and Biophysical Research CommunicationsRole of structural flexibility in the evolution of emerin
2015, Journal of Theoretical BiologyCitation Excerpt :High affinity between emerin and nuclear envelope protein nesprin was also reported (Mislow et al., 2002). In addition, emerin was shown to interact with splicing-associated factor YT521-B (Wilkinson et al., 2003), actin (Lattanzi et al., 2003), death-promoting transcriptional repressor Btf (Haraguchi et al., 2004), LIM domain containing protein Lmo7 (Holaska and Wilson, 2006), spermatogenesis associated protein GCL (Holaska et al., 2003), and many other proteins (Berk et al., 2013). Due to its specific cellular location and central role in interacting with many other important proteins, malfunction of emerin is directly associated with several serious human diseases.
Emerin in health and disease
2014, Seminars in Cell and Developmental BiologyCitation Excerpt :ERK2 directly phosphorylates emerin in vivo during lentiviral infection [202] and virally induced hyperphosphorylation causes altered distribution of emerin at the inner nuclear membrane and mislocalization of emerin to the outer nuclear membrane [201,204]. Emerin dephosphorylation occurs in vivo and protein phosphatase 1 activity weakens the interaction of emerin with nuclear actin [205]. Lambda phosphatase, a serine/threonine kinase, however, increased the interaction between emerin and actin [205], suggesting emerin-actin dynamics are regulated by distinct post-translational modifications in emerin.
A proteomic study of Hutchinson-Gilford progeria syndrome: Application of 2D-chromotography in a premature aging disease
2012, Biochemical and Biophysical Research CommunicationsCitation Excerpt :The nuclear lamina interacts with the nuclear pore complex, emerin, nesprins and SUN1 proteins. Emerin protein has been previously shown to interact with both α-actin-1 and β-tubulin [30], which have been found in this study to be differentially expressed in HGPS cells, in addition to binding with F-actin protein [31]. F-actin protein may bind directly with vimentin protein that was found in the present study to be up-regulated in HGPS cells.
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These authors contributed equally to this work.