RESUMEN

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.

Asunto(s)

Proteínas de Caenorhabditis elegans , Caenorhabditis elegans , Polaridad Celular , Distrofina , Músculos , Vía de Señalización Wnt , Animales , Caenorhabditis elegans/metabolismo , Proteínas de Caenorhabditis elegans/metabolismo , Proteínas de Caenorhabditis elegans/genética , Distrofina/metabolismo , Distrofina/genética , Músculos/metabolismo , Proteínas Dishevelled/metabolismo , Proteínas Dishevelled/genética , Receptores Huérfanos Similares al Receptor Tirosina Quinasa/metabolismo , Receptores Huérfanos Similares al Receptor Tirosina Quinasa/genética , Membrana Celular/metabolismo , Complejo de Proteínas Asociado a la Distrofina/metabolismo , Complejo de Proteínas Asociado a la Distrofina/genética , Proteínas Wnt/metabolismo , Transducción de Señal