Trafficking of Annexins during Membrane Repair in Human Skeletal Muscle Cells
Defects in membrane repair contribute to the development of muscular dystrophies, such as Miyoshi muscular dystrophy 1, limb girdle muscular dystrophy (LGMD), type R2 or R12. Deciphering membrane repair dysfunctions in the development of muscular dystrophies requires precise and detailed knowledge o...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-01-01
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| Series: | Membranes |
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| Online Access: | https://www.mdpi.com/2077-0375/12/2/153 |
| _version_ | 1827654000981311488 |
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| author | Coralie Croissant Céline Gounou Flora Bouvet Sisareuth Tan Anthony Bouter |
| author_facet | Coralie Croissant Céline Gounou Flora Bouvet Sisareuth Tan Anthony Bouter |
| author_sort | Coralie Croissant |
| collection | DOAJ |
| description | Defects in membrane repair contribute to the development of muscular dystrophies, such as Miyoshi muscular dystrophy 1, limb girdle muscular dystrophy (LGMD), type R2 or R12. Deciphering membrane repair dysfunctions in the development of muscular dystrophies requires precise and detailed knowledge of the membrane repair machinery in healthy human skeletal muscle cells. Using correlative light and electron microscopy (CLEM), we studied the trafficking of four members of the annexin (ANX) family, in myotubes damaged by laser ablation. Our data support a model in which ANXA4 and ANXA6 are recruited to the disruption site by propagating as a wave-like motion along the sarcolemma. They may act in membrane resealing by proceeding to sarcolemma remodeling. On the other hand, ANXA1 and A2 exhibit a progressive cytoplasmic recruitment, likely by interacting with intracellular vesicles, in order to form the lipid patch required for membrane resealing. Once the sarcolemma has been resealed, ANXA1 is released from the site of the membrane injury and returns to the cytosol, while ANXA2 remains accumulated close to the wounding site on the cytoplasmic side. On the other side of the repaired sarcolemma are ANXA4 and ANXA6 that face the extracellular milieu, where they are concentrated in a dense structure, the cap subdomain. The proposed model provides a basis for the identification of cellular dysregulations in the membrane repair of dystrophic human muscle cells. |
| first_indexed | 2024-03-09T21:28:30Z |
| format | Article |
| id | doaj.art-61f8f097468f4e2b9e67395ad92d3bf1 |
| institution | Directory Open Access Journal |
| issn | 2077-0375 |
| language | English |
| last_indexed | 2024-03-09T21:28:30Z |
| publishDate | 2022-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Membranes |
| spelling | doaj.art-61f8f097468f4e2b9e67395ad92d3bf12023-11-23T21:02:39ZengMDPI AGMembranes2077-03752022-01-0112215310.3390/membranes12020153Trafficking of Annexins during Membrane Repair in Human Skeletal Muscle CellsCoralie Croissant0Céline Gounou1Flora Bouvet2Sisareuth Tan3Anthony Bouter4Institute of Chemistry and Biology of Membranes and Nano-Objects, UMR 5248, CNRS, University of Bordeaux, IPB, F-33600 Pessac, FranceInstitute of Chemistry and Biology of Membranes and Nano-Objects, UMR 5248, CNRS, University of Bordeaux, IPB, F-33600 Pessac, FranceInstitute of Chemistry and Biology of Membranes and Nano-Objects, UMR 5248, CNRS, University of Bordeaux, IPB, F-33600 Pessac, FranceInstitute of Chemistry and Biology of Membranes and Nano-Objects, UMR 5248, CNRS, University of Bordeaux, IPB, F-33600 Pessac, FranceInstitute of Chemistry and Biology of Membranes and Nano-Objects, UMR 5248, CNRS, University of Bordeaux, IPB, F-33600 Pessac, FranceDefects in membrane repair contribute to the development of muscular dystrophies, such as Miyoshi muscular dystrophy 1, limb girdle muscular dystrophy (LGMD), type R2 or R12. Deciphering membrane repair dysfunctions in the development of muscular dystrophies requires precise and detailed knowledge of the membrane repair machinery in healthy human skeletal muscle cells. Using correlative light and electron microscopy (CLEM), we studied the trafficking of four members of the annexin (ANX) family, in myotubes damaged by laser ablation. Our data support a model in which ANXA4 and ANXA6 are recruited to the disruption site by propagating as a wave-like motion along the sarcolemma. They may act in membrane resealing by proceeding to sarcolemma remodeling. On the other hand, ANXA1 and A2 exhibit a progressive cytoplasmic recruitment, likely by interacting with intracellular vesicles, in order to form the lipid patch required for membrane resealing. Once the sarcolemma has been resealed, ANXA1 is released from the site of the membrane injury and returns to the cytosol, while ANXA2 remains accumulated close to the wounding site on the cytoplasmic side. On the other side of the repaired sarcolemma are ANXA4 and ANXA6 that face the extracellular milieu, where they are concentrated in a dense structure, the cap subdomain. The proposed model provides a basis for the identification of cellular dysregulations in the membrane repair of dystrophic human muscle cells.https://www.mdpi.com/2077-0375/12/2/153annexinmembrane repairskeletal musclecorrelative light and electron microscopy |
| spellingShingle | Coralie Croissant Céline Gounou Flora Bouvet Sisareuth Tan Anthony Bouter Trafficking of Annexins during Membrane Repair in Human Skeletal Muscle Cells Membranes annexin membrane repair skeletal muscle correlative light and electron microscopy |
| title | Trafficking of Annexins during Membrane Repair in Human Skeletal Muscle Cells |
| title_full | Trafficking of Annexins during Membrane Repair in Human Skeletal Muscle Cells |
| title_fullStr | Trafficking of Annexins during Membrane Repair in Human Skeletal Muscle Cells |
| title_full_unstemmed | Trafficking of Annexins during Membrane Repair in Human Skeletal Muscle Cells |
| title_short | Trafficking of Annexins during Membrane Repair in Human Skeletal Muscle Cells |
| title_sort | trafficking of annexins during membrane repair in human skeletal muscle cells |
| topic | annexin membrane repair skeletal muscle correlative light and electron microscopy |
| url | https://www.mdpi.com/2077-0375/12/2/153 |
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