A Dual Role for Actin and Microtubule Cytoskeleton in the Transport of Golgi Units from the Nurse Cells to the Oocyte Across Ring Canals

Nicolas, Émmanuelle; Chenouard, Nicolas; Olivo‐Marin, Jean‐Christophe; Guichet, Antoine

doi:10.1091/mbc.e08-04-0360

Cited by 31 publications

(31 citation statements)

References 53 publications

(69 reference statements)

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“…Multinucleation, indicating a defect in membrane stability, was first observed at the onset of vitellogenesis (stage 8). Loss of AP-1 never caused loss of oocyte membrane integrity, suggesting that this membrane is more robust than that of nurse cells, presumably because of its differential organization and composition (26).…”

Section: Significancementioning

confidence: 96%

Drosophila E-cadherin is required for the maintenance of ring canals anchoring to mechanically withstand tissue growth

Loyer

Kolotuev

Pinot

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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Intercellular bridges called "ring canals" (RCs) resulting from incomplete cytokinesis play an essential role in intercellular communication in somatic and germinal tissues. During Drosophila oogenesis, RCs connect the maturing oocyte to nurse cells supporting its growth. Despite numerous genetic screens aimed at identifying genes involved in RC biogenesis and maturation, how RCs anchor to the plasma membrane (PM) throughout development remains unexplained. In this study, we report that the clathrin adaptor protein 1 (AP-1) complex, although dispensable for the biogenesis of RCs, is required for the maintenance of the anchorage of RCs to the PM to withstand the increased membrane tension associated with the exponential tissue growth at the onset of vitellogenesis. Here we unravel the mechanisms by which AP-1 enables the maintenance of RCs' anchoring to the PM during size expansion. We show that AP-1 regulates the localization of the intercellular adhesion molecule E-cadherin and that loss of AP-1 causes the disappearance of the E-cadherin-containing adhesive clusters surrounding the RCs. E-cadherin itself is shown to be required for the maintenance of the RCs' anchorage, a function previously unrecognized because of functional compensation by N-cadherin. Scanning block-face EM combined with transmission EM analyses reveals the presence of interdigitated, actin-and Moesin-positive, microvilli-like structures wrapping the RCs. Thus, by modulating E-cadherin trafficking, we show that the sustained E-cadherin-dependent adhesion organizes the microvilli meshwork and ensures the proper attachment of RCs to the PM, thereby counteracting the increasing membrane tension induced by exponential tissue growth.

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Section: Significancementioning

confidence: 96%

Drosophila E-cadherin is required for the maintenance of ring canals anchoring to mechanically withstand tissue growth

Loyer

Kolotuev

Pinot

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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“…( C ) Morphology of a wild-type ring canal revealed by staining for F-actin and HTS r.c. Note the very regular ring form and the actin filaments extending from the ring canal (“actin basket”) (Nicolas et al, 2009). Scale bar represents 2.5 µm.…”

Section: Resultsmentioning

confidence: 99%

Drosophilasosiefunctions with βH-Spectrin and actin organizers in cell migration, epithelial morphogenesis and cortical stability

2012

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SummaryMorphogenesis in multicellular organisms requires the careful coordination of cytoskeletal elements, dynamic regulation of cell adhesion and extensive cell migration. sosie (sie) is a novel gene required in various morphogenesis processes in Drosophila oogenesis. Lack of sie interferes with normal egg chamber packaging, maintenance of epithelial integrity and control of follicle cell migration, indicating that sie is involved in controlling epithelial integrity and cell migration. For these functions sie is required both in the germ line and in the soma. Consistent with this, Sosie localizes to plasma membranes in the germ line and in the somatic follicle cells and is predicted to present an EGF-like domain on the extracellular side. Two positively charged residues, C-terminal to the predicted transmembrane domain (on the cytoplasmic side), are required for normal plasma membrane localization of Sosie. Because sie also contributes to normal cortical localization of βH-Spectrin, it appears that cortical βH-Spectrin mediates some of the functions of sosie. sie also interacts with the genes coding for the actin organizers Filamin and Profilin and, in the absence of sie function, F-actin is less well organized and nurse cells frequently fuse.

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“…2B), cytoplasmic bridges that connect the cells of a germline cyst. Ring canals consist of a dense inner ring of bipolar actin filaments and an associated crown and fishing-weir-like basket of needle-like actin bundles (Nicolas et al, 2009; reviewed by Hudson and Cooley, 2002). Myo7A was strongly enriched at the crown (Fig.…”

Section: Myo7a Associates With Parallel Bundles Of Actin Filaments Dumentioning

confidence: 98%

Myosin VIIA regulates microvillus morphogenesis and interacts with cadherin Cad99C in Drosophila oogenesis

et al. 2014

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BSTRACTMicrovilli and related actin-based protrusions permit multiple interactions between cells and their environment. How the shape, length and arrangement of microvilli are determined remains largely unclear. To address this issue and explore the cooperation of the two main components of a microvillus, the central F-actin bundle and the enveloping plasma membrane, we investigated the expression and function of Myosin VIIA (Myo7A), which is encoded by crinkled (ck), and its interaction with cadherin Cad99C in the microvilli of the Drosophila follicular epithelium. Myo7A is present in the microvilli and terminal web of follicle cells, and associates with several other F-actin-rich structures in the ovary. Loss of Myo7A caused brush border defects and a reduction in the amount of the microvillus regulator Cad99C. We show that Myo7A and Cad99C form a molecular complex and that the cytoplasmic tail of Cad99C recruits Myo7A to microvilli. Our data indicate that Myo7A regulates the structure and spacing of microvilli, and interacts with Cad99C in vivo. A comparison of the mutant phenotypes suggests that Myo7A and Cad99C have co-dependent and independent functions in microvilli.

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A Dual Role for Actin and Microtubule Cytoskeleton in the Transport of Golgi Units from the Nurse Cells to the Oocyte Across Ring Canals

Cited by 31 publications

References 53 publications

Drosophila E-cadherin is required for the maintenance of ring canals anchoring to mechanically withstand tissue growth

Drosophila E-cadherin is required for the maintenance of ring canals anchoring to mechanically withstand tissue growth

Drosophilasosiefunctions with βH-Spectrin and actin organizers in cell migration, epithelial morphogenesis and cortical stability

Myosin VIIA regulates microvillus morphogenesis and interacts with cadherin Cad99C in Drosophila oogenesis

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