Organization of the apical extracellular matrix during tubular organ formation DOI Creative Commons

Jennifer Woodward,

Jeffrey Matthew, Vishakha Vishwakarma

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2024, Volume and Issue: unknown

Published: Nov. 21, 2024

The apical extracellular matrix (aECM) plays a critical role in epithelial tube morphogenesis during organ formation, but its composition and organization remain poorly understood. Using the Drosophila embryonic salivary gland (SG) as model, we identify Papss, an enzyme that synthesizes universal sulfate donor PAPS, regulator of lumen expansion. Papss mutants show disorganized membrane, condensed aECM, disruptions Golgi structures intracellular trafficking. Additionally, two zona pellucida (ZP) domain proteins, Piopio (Pio) Dumpy (Dpy), key components SG aECM. In absence Pio is gradually lost while Dpy-positive aECM structure dissociates from leading to thin lumen. Mutations dpy or pio, Notopleural, which encodes matriptase cleaves form luminal pool, result with alternating bulges constrictions, loss pio Dpy Our findings underscore essential sulfation organizing tubular formation highlight mechanical support provided by ZP proteins maintaining diameter.

Language: Английский

Organization of the apical extracellular matrix during tubular organ formation DOI Creative Commons

Jennifer Woodward,

Jeffrey Matthew, Vishakha Vishwakarma

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2024, Volume and Issue: unknown

Published: Nov. 21, 2024

The apical extracellular matrix (aECM) plays a critical role in epithelial tube morphogenesis during organ formation, but its composition and organization remain poorly understood. Using the Drosophila embryonic salivary gland (SG) as model, we identify Papss, an enzyme that synthesizes universal sulfate donor PAPS, regulator of lumen expansion. Papss mutants show disorganized membrane, condensed aECM, disruptions Golgi structures intracellular trafficking. Additionally, two zona pellucida (ZP) domain proteins, Piopio (Pio) Dumpy (Dpy), key components SG aECM. In absence Pio is gradually lost while Dpy-positive aECM structure dissociates from leading to thin lumen. Mutations dpy or pio, Notopleural, which encodes matriptase cleaves form luminal pool, result with alternating bulges constrictions, loss pio Dpy Our findings underscore essential sulfation organizing tubular formation highlight mechanical support provided by ZP proteins maintaining diameter.

Language: Английский

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