Fer1L5, a Dysferlin Homologue Present in Vesicles and Involved in C2C12 Myoblast Fusion and Membrane Repair
Fer1L5 is a dysferlin and myoferlin related protein, which has been predicted to have a role in vesicle trafficking and muscle membrane fusion events. Mutations in dysferlin and otoferlin genes cause heredity diseases: muscular dystrophy and deafness in humans, respectively. Dysferlin is implicated...
| Main Authors: | , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2020-11-01
|
| Series: | Biology |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2079-7737/9/11/386 |
| _version_ | 1797548451854024704 |
|---|---|
| author | R. Usha Kalyani K. Perinbam P. Jeyanthi Naif Abdullah Al-Dhabi Mariadhas Valan Arasu Galal Ali Esmail Young Ock Kim Hyungsuk Kim Hak-Jae Kim |
| author_facet | R. Usha Kalyani K. Perinbam P. Jeyanthi Naif Abdullah Al-Dhabi Mariadhas Valan Arasu Galal Ali Esmail Young Ock Kim Hyungsuk Kim Hak-Jae Kim |
| author_sort | R. Usha Kalyani |
| collection | DOAJ |
| description | Fer1L5 is a dysferlin and myoferlin related protein, which has been predicted to have a role in vesicle trafficking and muscle membrane fusion events. Mutations in dysferlin and otoferlin genes cause heredity diseases: muscular dystrophy and deafness in humans, respectively. Dysferlin is implicated in membrane repair. Myoferlin has a role in myogenesis. In this study, we investigated the role of the Fer1L5 protein during myoblast fusion and membrane repair. To study the functions of Fer1L5 we used confocal microscopy, biochemical fractionation, Western blot analysis and multiphoton laser wounding assay. By immunolabelling, Fer1L5 was detected in vesicular structures. By biochemical fractionation Fer1L5 was observed in low density vesicles. Our studies show that the membranes of Fer1L5 vesicles are non-resistant to non-ionic detergent. Partial co-staining of Fer1L5 with other two ferlin vesicles, respectively, was observed. Fer1L5 expression was highly detected at the fusion sites of two apposed C2C12 myoblast membranes and its expression level gradually increased at D2 and reached a maximum at day 4 before decreasing during further differentiation. Our studies showed that Fer1L5 has fusion defects during myoblast fusion and impaired membrane repair when the C2C12 cultures were incubated with inhibitory Fer1L5 antibodies. In C2C12 cells Fer1L5 vesicles are involved in two stages, the fusion of myoblasts and the formation of large myotubes. Fer1L5 also plays a role in membrane repair. |
| first_indexed | 2024-03-10T14:59:31Z |
| format | Article |
| id | doaj.art-17a3b5cdca734c3a946c700947ad9254 |
| institution | Directory Open Access Journal |
| issn | 2079-7737 |
| language | English |
| last_indexed | 2024-03-10T14:59:31Z |
| publishDate | 2020-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biology |
| spelling | doaj.art-17a3b5cdca734c3a946c700947ad92542023-11-20T20:13:57ZengMDPI AGBiology2079-77372020-11-0191138610.3390/biology9110386Fer1L5, a Dysferlin Homologue Present in Vesicles and Involved in C2C12 Myoblast Fusion and Membrane RepairR. Usha Kalyani0K. Perinbam1P. Jeyanthi2Naif Abdullah Al-Dhabi3Mariadhas Valan Arasu4Galal Ali Esmail5Young Ock Kim6Hyungsuk Kim7Hak-Jae Kim8PG and Research Department of Botany, Government Arts College for Men (Autonomous), Affiliated to Univerity of Madras, Chennai 600035, IndiaPG and Research Department of Botany, Government Arts College for Men (Autonomous), Affiliated to Univerity of Madras, Chennai 600035, IndiaSathyabama Institute of Science and Technology, Chennai 600119, IndiaDepartment of Botany and Microbiology, College of Science, King Saud University, P.O. Box 2455, Riyadh 11451, Saudi ArabiaDepartment of Botany and Microbiology, College of Science, King Saud University, P.O. Box 2455, Riyadh 11451, Saudi ArabiaDepartment of Botany and Microbiology, College of Science, King Saud University, P.O. Box 2455, Riyadh 11451, Saudi ArabiaDepartment of Clinical Pharmacology, College of Medicine, Soonchunhyang University, Cheonan 31538, KoreaDepartment of Rehabilitation Medicine of Korean Medicine, College of Korean Medicine, Kyung Hee University, Seoul 02447, KoreaDepartment of Clinical Pharmacology, College of Medicine, Soonchunhyang University, Cheonan 31538, KoreaFer1L5 is a dysferlin and myoferlin related protein, which has been predicted to have a role in vesicle trafficking and muscle membrane fusion events. Mutations in dysferlin and otoferlin genes cause heredity diseases: muscular dystrophy and deafness in humans, respectively. Dysferlin is implicated in membrane repair. Myoferlin has a role in myogenesis. In this study, we investigated the role of the Fer1L5 protein during myoblast fusion and membrane repair. To study the functions of Fer1L5 we used confocal microscopy, biochemical fractionation, Western blot analysis and multiphoton laser wounding assay. By immunolabelling, Fer1L5 was detected in vesicular structures. By biochemical fractionation Fer1L5 was observed in low density vesicles. Our studies show that the membranes of Fer1L5 vesicles are non-resistant to non-ionic detergent. Partial co-staining of Fer1L5 with other two ferlin vesicles, respectively, was observed. Fer1L5 expression was highly detected at the fusion sites of two apposed C2C12 myoblast membranes and its expression level gradually increased at D2 and reached a maximum at day 4 before decreasing during further differentiation. Our studies showed that Fer1L5 has fusion defects during myoblast fusion and impaired membrane repair when the C2C12 cultures were incubated with inhibitory Fer1L5 antibodies. In C2C12 cells Fer1L5 vesicles are involved in two stages, the fusion of myoblasts and the formation of large myotubes. Fer1L5 also plays a role in membrane repair.https://www.mdpi.com/2079-7737/9/11/386Fer1L5dysferlinmyoferlinvesiclesmyoblast fusionmembrane repair |
| spellingShingle | R. Usha Kalyani K. Perinbam P. Jeyanthi Naif Abdullah Al-Dhabi Mariadhas Valan Arasu Galal Ali Esmail Young Ock Kim Hyungsuk Kim Hak-Jae Kim Fer1L5, a Dysferlin Homologue Present in Vesicles and Involved in C2C12 Myoblast Fusion and Membrane Repair Biology Fer1L5 dysferlin myoferlin vesicles myoblast fusion membrane repair |
| title | Fer1L5, a Dysferlin Homologue Present in Vesicles and Involved in C2C12 Myoblast Fusion and Membrane Repair |
| title_full | Fer1L5, a Dysferlin Homologue Present in Vesicles and Involved in C2C12 Myoblast Fusion and Membrane Repair |
| title_fullStr | Fer1L5, a Dysferlin Homologue Present in Vesicles and Involved in C2C12 Myoblast Fusion and Membrane Repair |
| title_full_unstemmed | Fer1L5, a Dysferlin Homologue Present in Vesicles and Involved in C2C12 Myoblast Fusion and Membrane Repair |
| title_short | Fer1L5, a Dysferlin Homologue Present in Vesicles and Involved in C2C12 Myoblast Fusion and Membrane Repair |
| title_sort | fer1l5 a dysferlin homologue present in vesicles and involved in c2c12 myoblast fusion and membrane repair |
| topic | Fer1L5 dysferlin myoferlin vesicles myoblast fusion membrane repair |
| url | https://www.mdpi.com/2079-7737/9/11/386 |
| work_keys_str_mv | AT rushakalyani fer1l5adysferlinhomologuepresentinvesiclesandinvolvedinc2c12myoblastfusionandmembranerepair AT kperinbam fer1l5adysferlinhomologuepresentinvesiclesandinvolvedinc2c12myoblastfusionandmembranerepair AT pjeyanthi fer1l5adysferlinhomologuepresentinvesiclesandinvolvedinc2c12myoblastfusionandmembranerepair AT naifabdullahaldhabi fer1l5adysferlinhomologuepresentinvesiclesandinvolvedinc2c12myoblastfusionandmembranerepair AT mariadhasvalanarasu fer1l5adysferlinhomologuepresentinvesiclesandinvolvedinc2c12myoblastfusionandmembranerepair AT galalaliesmail fer1l5adysferlinhomologuepresentinvesiclesandinvolvedinc2c12myoblastfusionandmembranerepair AT youngockkim fer1l5adysferlinhomologuepresentinvesiclesandinvolvedinc2c12myoblastfusionandmembranerepair AT hyungsukkim fer1l5adysferlinhomologuepresentinvesiclesandinvolvedinc2c12myoblastfusionandmembranerepair AT hakjaekim fer1l5adysferlinhomologuepresentinvesiclesandinvolvedinc2c12myoblastfusionandmembranerepair |