Morphological study of TNPO3 and SRSF1 interaction during myogenesis by combining confocal,structured illumination and electron microscopy analysis |
| |
Authors: | Costa Roberta Rodia Maria Teresa Zini Nicoletta Pegoraro Valentina Marozzo Roberta Capanni Cristina Angelini Corrado Lattanzi Giovanna Santi Spartaco Cenacchi Giovanna |
| |
Affiliation: | 1.Department of Biomedical and Neuromotor Sciences—DIBINEM, Alma Mater Studiorum University of Bologna, via Massarenti 9, 40138, Bologna, Italy ;2.Center of Applied Biomedical Research—CRBA, Alma Mater Studiorum University of Bologna, St. Orsola Hospital, via Massarenti 9, 40138, Bologna, Italy ;3.CNR—National Research Council of Italy, Institute of Molecular Genetics “Luigi Luca Cavalli-Sforza”, Unit of Bologna, via di Barbiano 1/10, 40136, Bologna, Italy ;4.IRCCS Istituto Ortopedico Rizzoli, via di Barbiano 1/10, 40136, Bologna, Italy ;5.Neuromuscular Unit, Neurobiology Research group, IRCCS San Camillo Hospital, via Alberoni 70, 30126, Venice, Italy ; |
| |
Abstract: | Transportin3 (TNPO3) shuttles the SR proteins from the cytoplasm to the nucleus. The SR family includes essential splicing factors, such as SRSF1, that influence alternative splicing, controlling protein diversity in muscle and satellite cell differentiation. Given the importance of alternative splicing in the myogenic process and in the maintenance of healthy muscle, alterations in the splicing mechanism might contribute to the development of muscle disorders. Combining confocal, structured illumination and electron microscopy, we investigated the expression of TNPO3 and SRSF1 during myogenesis, looking at nuclear and cytoplasmic compartments. We investigated TNPO3 and its interaction with SRSF1 and we observed that SRSF1 remained mainly localized in the nucleus, while TNPO3 decreased in the cytoplasm and was strongly clustered in the nuclei of differentiated myotubes. In conclusion, combining different imaging techniques led us to describe the behavior of TNPO3 and SRSF1 during myogenesis, showing that their dynamics follow the myogenic process and could influence the proteomic network necessary during myogenesis. The combination of different high-, super- and ultra-resolution imaging techniques led us to describe the behavior of TNPO3 and its interaction with SRSF1, looking at nuclear and cytoplasmic compartments. These observations represent a first step in understanding the role of TNPO3 and SRFSF1 in complex mechanisms, such as myogenesis. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|