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Nat Commun ; 15(1): 4935, 2024 Jun 10.
Artigo em Inglês | MEDLINE | ID: mdl-38858388

RESUMO

Cell polarity mechanisms allow the formation of specialized membrane domains with unique protein compositions, signalling properties, and functional characteristics. By analyzing the localization of potassium channels and proteins belonging to the dystrophin-associated protein complex, we reveal the existence of distinct planar-polarized membrane compartments at the surface of C. elegans muscle cells. We find that muscle polarity is controlled by a non-canonical Wnt signalling cascade involving the ligand EGL-20/Wnt, the receptor CAM-1/Ror, and the intracellular effector DSH-1/Dishevelled. Interestingly, classical planar cell polarity proteins are not required for this process. Using time-resolved protein degradation, we demonstrate that -while it is essentially in place by the end of embryogenesis- muscle polarity is a dynamic state, requiring continued presence of DSH-1 throughout post-embryonic life. Our results reveal the unsuspected complexity of the C. elegans muscle membrane and establish a genetically tractable model system to study cellular polarity and membrane compartmentalization in vivo.


Assuntos
Proteínas de Caenorhabditis elegans , Caenorhabditis elegans , Polaridade Celular , Distrofina , Músculos , Via de Sinalização Wnt , Animais , Caenorhabditis elegans/metabolismo , Proteínas de Caenorhabditis elegans/metabolismo , Proteínas de Caenorhabditis elegans/genética , Distrofina/metabolismo , Distrofina/genética , Músculos/metabolismo , Proteínas Desgrenhadas/metabolismo , Proteínas Desgrenhadas/genética , Receptores Órfãos Semelhantes a Receptor Tirosina Quinase/metabolismo , Receptores Órfãos Semelhantes a Receptor Tirosina Quinase/genética , Membrana Celular/metabolismo , Complexo de Proteínas Associadas Distrofina/metabolismo , Complexo de Proteínas Associadas Distrofina/genética , Proteínas Wnt/metabolismo , Transdução de Sinais
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