UNASSIGNED: @entity2199 embryonic elongation is a morphogenetic event driven by actomyosin contractility and muscle-induced tension transmitted through hemidesmosomes. A role for the microtubule cytoskeleton has also been proposed, but its contribution remains poorly characterized. Here, we investigate the organization of the non-centrosomal microtubule arrays present in the epidermis and assess their function in elongation. We show that the microtubule regulators y-tubulin and @entity69164 are recruited to hemidesmosomes and adherens junctions early in elongation. Several parallel approaches suggest that microtubule nucleation occurs from these sites. Disrupting the epidermal microtubule array by overexpressing the microtubule-severing protein Spastin or by inhibiting the @entity2199 ninein homolog @entity69164 in the epidermis mildly affected elongation. However, microtubules were essential for elongation when hemidesmosomes or the activity of the Rho-kinase @entity69165 /ROCK were partially compromised. Imaging of junctional components and genetic analyses suggest that epidermal microtubules function together with Rho-kinase to promote the transport of E-cadherin to adherens junctions and myotactin to hemidesmosomes. Our results indicate that @entity69165 /ROCK role in junctional remodeling is likely independent of its established function as a myosin II activator, but requires a microtubule-dependent pathway involving the syntaxin SYX-5. Hence, we propose that non-centrosomal microtubules organized by epidermal junctions contribute to elongation by transporting junction remodeling factors, rather than having a mechanical role.

Non-centrosomal epidermal microtubules act in parallel to XXXX /ROCK to promote @entity2199 elongation.

@entity69165 :: ('172088(Tax:6239)', 'Gene') :: ['LET-502'] @entity2199 :: ('6239', 'Species') :: ['C. elegans'] @entity69164 :: ('3565610(Tax:6239)', 'Gene') :: ['NOCA-1']
@entity69165 :: (172088(Tax:6239),Gene) :: ['LET-502']
