Defective membrane repair machinery impairs survival of invasive cancer cells

Bouvet, Flora; Ros, Manon; Bonedeau, E.; Croissant, Coralie; Frelin, Léo; Saltel, Frédéric; Moreau, Violaine; Bouter, Anthony

doi:10.1038/s41598-020-77902-5

Cited by 22 publications

(28 citation statements)

References 70 publications

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“…Membrane damage was performed by laser ablation as previously described [17,26]. Briefly, myotubes were formed and cultured in a 35-mm glass bottom dish equipped with a square-patterned coverslip (MatTek, Ashland, MA, USA).…”

Section: Subcellular Trafficking Of Anx Fused To Fluorescent Proteins...mentioning

confidence: 99%

Trafficking of Annexins during Membrane Repair in Human Skeletal Muscle Cells

et al. 2022

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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.

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Section: Subcellular Trafficking Of Anx Fused To Fluorescent Proteins...mentioning

confidence: 99%

Trafficking of Annexins during Membrane Repair in Human Skeletal Muscle Cells

et al. 2022

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“…During cytokinesis, actin filaments are bundled and stabilized against the plasma membrane, and mammalian Annexin A2-depleted cells show defects in cytokinesis [ 33 , 34 ]. Mammalian Annexins are also required for proper cell wound repair, facilitating the spatial localization of proteins such as dysferlin in muscle cells [ 24 , 35 , 36 , 37 , 38 , 39 , 40 , 41 ]. In the Drosophila model, Annexin B9 is rapidly (<3 s) recruited to wounds to stabilize actin.…”

Section: Actin Ring Formationmentioning

confidence: 99%

“…One such protein family, Annexins, are fast-responding calcium-regulated proteins that mediate cytoskeleton stabilization and cell cortex remodeling, and whose expression is often upregulated in response to injury [ 27 , 32 , 33 , 35 , 38 ]. Different Annexins have been shown to affect many aspects of the cell wound repair process, ranging from their effects on actin architecture and organization to the modulation of cortical tension associated with bringing wound edges together [ 27 , 36 , 37 , 39 , 124 , 125 , 126 ].…”

Section: Relationship To Diseases and Infectionsmentioning

confidence: 99%

Wrangling Actin Assemblies: Actin Ring Dynamics during Cell Wound Repair

Hui

Stjepić

Nakamura

et al. 2022

Cells

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To cope with continuous physiological and environmental stresses, cells of all sizes require an effective wound repair process to seal breaches to their cortex. Once a wound is recognized, the cell must rapidly plug the injury site, reorganize the cytoskeleton and the membrane to pull the wound closed, and finally remodel the cortex to return to homeostasis. Complementary studies using various model organisms have demonstrated the importance and complexity behind the formation and translocation of an actin ring at the wound periphery during the repair process. Proteins such as actin nucleators, actin bundling factors, actin-plasma membrane anchors, and disassembly factors are needed to regulate actin ring dynamics spatially and temporally. Notably, Rho family GTPases have been implicated throughout the repair process, whereas other proteins are required during specific phases. Interestingly, although different models share a similar set of recruited proteins, the way in which they use them to pull the wound closed can differ. Here, we describe what is currently known about the formation, translocation, and remodeling of the actin ring during the cell wound repair process in model organisms, as well as the overall impact of cell wound repair on daily events and its importance to our understanding of certain diseases and the development of therapeutic delivery modalities.

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“…Our novel approach allows us to test the cellular response to PM ruptures of nanoscopic dimensions in both cells and model membranes. Nanoscopic holes of this dimension may be frequently occurring during aggressive cellular migration and invasion 1,30 and therefore investigation of protein recruitment in response to nanoscopic ruptures are relevant for understanding how living cells cope with ruptures.…”

Section: Resultsmentioning

confidence: 99%