Rac1 controls epithelial tube length through the apical secretion and polarity pathways

Sollier, Kévin; Gaudé, Helori-Mael; Chartier, François; Laprise, Patrick

doi:10.1242/bio.015727

Cited by 13 publications

(13 citation statements)

References 36 publications

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“…Following this logic, overexpressed βPS integrin would then also be trafficked through a different route from that of the endogenous βPS integrin, possibly because of higher expression levels or because of the presence of the Venus fused to the normal protein. Another reason for the sensitivity of Crb to loss of Tango1 may be that it is intensively recycled from the plasma membrane in tracheal cells and other tissues (Roeth et al, 2009; Schottenfeld-Roames et al, 2014; Sollier et al, 2015). We may therefore be seeing recycling Crb being trapped as a secondary consequence of the defects in the ER and Golgi system, whereas βPS integrin might remain in the plasma membrane once it has reached the cell surface, and therefore be able to gradually assembly there to near-normal levels even when it is partly blocked in its transit.…”

Section: Discussionmentioning

confidence: 99%

Dual function for Tango1 in secretion of bulky cargo and in ER-Golgi morphology

Ríos-Barrera

Sigurbjörnsdóttir

Baer

et al. 2017

Preprint

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Tango1 helps the efficient delivery of large proteins to the cell surface. We show here that loss of Tango1, in addition to interfering with protein secretion, causes ER stress and defects in cell and ER/Golgi morphology. We find that the previously observed dependence of smaller cargos on Tango1 is a secondary effect, due to an indirect requirement: if large cargos like Dumpy, which we identify here as a new Tango1 cargo, are removed from the cell, non-bulky proteins re-enter the secretory pathway. Removal of the blocking cargo also attenuates the ER-stress response, and cell morphology is restored. Thus, failures in the secretion of non-bulky proteins, ER stress and defective cell morphology are secondary consequences of the retention of cargo. By contrast, the ERES defects in Tango1-depleted cells persist in the absence of bulky cargo, showing that they are due to a secretion-independent function of Tango1. Therefore, the maintenance of proper ERES architecture may be a primary function for Tango1.

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Section: Discussionmentioning

confidence: 99%

Dual function for Tango1 in secretion of bulky cargo and in ER-Golgi morphology

Ríos-Barrera

Sigurbjörnsdóttir

Baer

et al. 2017

Preprint

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“…Normal ECs in Drosophila midgut have a welldefined basal-apical polarity, and many polarity proteins and junction proteins are localized to the apical side toward the lumen (Jiang et al 2009;Liang et al 2017). One of these polarity proteins Coracle can be detected as well-defined, tight staining near the apical/luminal side of ECs ( Figure 2A) (Laprise et al 2009;Sollier et al 2015). In the Myo1A .…”

Section: The Apical Localization Of Coracle Is Defective After Loss Omentioning

confidence: 99%

Oncogenic Pathways and Loss of the Rab11 GTPase Synergize To Alter Metabolism in Drosophila

Nie

et al. 2019

Genetics

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Colorectal cancer is a complex disease driven by well-established mutations such as APC and other yet to be identified pathways. The GTPase Rab11 regulates endosomal protein trafficking, and previously we showed that loss of Rab11 caused intestinal inflammation and hyperplasia in mice and flies. To test the idea that loss of Rab11 may promote cancer progression, we have analyzed archival human patient tissues and observed that 51 out of 70 colon cancer tissues had lower Rab11 protein staining. By using the Drosophila midgut model, we have found that loss of Rab11 can lead to three changes that may relate to cancer progression. First is the disruption of enterocyte polarity based on staining of the FERM domain protein Coracle. Second is an increased proliferation due to an increased expression of the JAK-STAT pathway ligand Upd3. Third is an increased expression of ImpL2, which is an IGFBP7 homolog and can suppress metabolism. Furthermore, loss of Rab11 can act synergistically with the oncoprotein Ras V12 to regulate these cancerrelated phenotypes.

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“…More specifically, it has been reported that Yurt and Coracle regulate tube size through the apical polarity protein Crumbs, while Scribble possibly achieves tube‐size regulation through other proteins 45 . More recently, the small GTPase Rac1 (FlyBase ID:FBgn0010333) has been shown to act as a basic regulator of epithelial tube morphogenesis through a positive feedback loop with Coracle and promotion of crumbs endocytosis 46 …”

Section: Current Evidence and Integration Of Findingsmentioning

confidence: 99%

The Drosophila septate junctions beyond barrier function: Review of the literature, prediction of human orthologs of the SJ‐related proteins and identification of protein domain families

et al. 2020

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The involvement of Septate Junctions (SJs) in critical cellular functions that extend beyond their role as diffusion barriers in the epithelia and the nervous system has made the fruit fly an ideal model for the study of human diseases associated with impaired Tight Junction (TJ) function. In this study, we summarized current knowledge of the Drosophila melanogaster SJ‐related proteins, focusing on their unconventional functions. Additionally, we sought to identify human orthologs of the corresponding genes as well as protein domain families. The systematic literature search was performed in PubMed and Scopus databases using relevant key terms. Orthologs were predicted using the DIOPT tool and aligned protein regions were determined from the Pfam database. 3‐D models of the smooth SJ proteins were built on the Phyre2 and DMPFold protein structure prediction servers. A total of 30 proteins were identified as relatives to the SJ cellular structure. Key roles of these proteins, mainly in the regulation of morphogenetic events and cellular signalling, were highlighted. The investigation of protein domain families revealed that the SJ‐related proteins contain conserved domains that are required not only for cell‐cell interactions and cell polarity but also for cellular signalling and immunity. DIOPT analysis of orthologs identified novel human genes as putative functional homologs of the fruit fly SJ genes. A gap in our knowledge was identified regarding the domains that occur in the proteins encoded by eight SJ‐associated genes. Future investigation of these domains is needed to provide functional information.

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Rac1 controls epithelial tube length through the apical secretion and polarity pathways

Cited by 13 publications

References 36 publications

Dual function for Tango1 in secretion of bulky cargo and in ER-Golgi morphology

Dual function for Tango1 in secretion of bulky cargo and in ER-Golgi morphology

Oncogenic Pathways and Loss of the Rab11 GTPase Synergize To Alter Metabolism in Drosophila

The Drosophila septate junctions beyond barrier function: Review of the literature, prediction of human orthologs of the SJ‐related proteins and identification of protein domain families

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