Stratum, a Homolog of the Human GEF Mss4, Partnered with Rab8, Controls the Basal Restriction of Basement Membrane Proteins in Epithelial Cells

Devergne, Olivier; Sun, Gina H.; Schüpbach, Trudi

doi:10.1016/j.celrep.2017.02.002

Cited by 33 publications

(44 citation statements)

References 31 publications

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“…We found that AP-1 and Strat act redundantly to control the basolateral targeting of Notch, Delta and Spdo in SOP daughter cells explaining the partial compensation of one by the other. These results are in agreement with previous studies demonstrating the involvement of Rab8, whose activity and localization is controlled by Strat in Drosophila (Bellec et al, 2018;Devergne et al, 2017), in the basolateral sorting of proteins (Ang et al, 2003;Henry and Sheff, 2008;Huber et al, 1993).…”

Section: Strat and Ap-1 Act Redundantly In The Basolateral Transport supporting

confidence: 94%

Clathrin adaptor AP-1 and Stratum act in parallel pathways to control Notch activation inDrosophilaSensory Organ Precursor Cells

Bellec

Pinot

Gicquel

et al. 2020

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Drosophila sensory organ precursors divide asymmetrically to generate pIIa/pIIb cells whose identity relies on the differential activation of Notch at cytokinesis. While Notch is present apically and basally relative to the midbody at the pIIa-pIIb interface, only the basal pool of Notch is reported to contribute to Notch activation in the pIIa cell. Correct intra-lineage signalling requires appropriate apico-basal targeting of Notch, its ligand Delta and its trafficking partner Sanpodo. We previously reported that AP-1 and Stratum regulate the intracellular trafficking of Notch and Sanpodo from the trans-Golgi network to the basolateral membrane. Loss of AP-1 or Stratum caused mild Notch gain-of-function phenotypes. Here, we report that the concomitant loss of AP-1 and Stratum results in a much more penetrant Notch gain-of-function phenotype indicating that AP-1 and Strat control two parallel pathways. While unequal partitioning of cell fate determinants and cell polarity were unaffected, Numb-mediated symmetry breaking is impaired. We further observed increased amounts of signaling competent Notch as well as Delta and Sanpodo at the apical pIIa-pIIb interface and the loss of the basal pool of Notch. We propose that AP-1 and Stratum operate in two parallel pathways to ensure the correct apico-basal localization of Notch controlling where receptor activation takes place.

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Section: Strat and Ap-1 Act Redundantly In The Basolateral Transport supporting

confidence: 94%

Clathrin adaptor AP-1 and Stratum act in parallel pathways to control Notch activation inDrosophilaSensory Organ Precursor Cells

Bellec

Pinot

Gicquel

et al. 2020

Preprint

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“…We then wondered whether BM fibril deposition is affected in Dys and Dg mutants. In these two mutants, the general targeting of BM secretion towards the basal domain is normal, with no visible apical secretion as it has been observed in different mutants affecting BM secretion (Denef et al, 2008;Devergne et al, 2014;Lerner et al, 2013;Devergne et al, 2017). However, images in the focal plane of the BM reveal a very strong decrease of the ColIV-fibrils in Dys null mutant ( Fig.…”

Section: The Dapc Is Important For Bm Fibril Depositionsupporting

confidence: 56%

Oriented basement membrane fibrils provide a memory for F-actin planar polarization via the Dystrophin-Dystroglycan complex during tissue elongation

campos

Alégot

Dennis

et al. 2019

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How extracellular matrix participates to tissue morphogenesis is still an open question. In the Drosophila ovarian follicle, it has been proposed that after Fat2-dependent planar polarization of the follicle cell basal domain, oriented basement membrane (BM) fibrils and F-actin stress fibers constrain follicle growth, promoting its axial elongation. However, the relationship between BM fibrils and stress fibers and their respective impact on elongation are unclear. We found that Dystroglycan (Dg) and Dystrophin (Dys) are involved in BM fibril deposition. Moreover, they orient stress fibers, by acting locally and in parallel to Fat2. Nonetheless, Dg-Dys complex-mediated cell autonomous control of Factin fibers orientation relies on the previous BM fibril deposition, indicating two distinct but interdependent functions. Thus, the Dg-Dys complex works as a critical organizer of the epithelial basal domain, regulating both F-actin and BM. Furthermore, BM fibrils act as a persistent cue for the orientation of stress fibers that are the main effector of elongation.

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“…Chemical inhibition or genetic ablation of Pten in Crb-deficient glands not only suppresses the formation of PAMS, but also restores the apical pools of Rab11, Rab30, apical secretion, larval food intake and timely pupariation. The relevance of PI(4,5)P 2 levels for proper secretion is highlighted by recent results demonstrating that the activity of Drosophila Crag (a Rab10 GEF) and Stratum (a Rab8 GEF) is regulated by the levels of PI(4,5)P 2 (Devergne et al, 2014; 2017). For example, in the follicle epithelium, reduction of PI(4,5)P 2 levels results in defective secretion of basal membrane proteins, which then accumulate at the apical membrane (Devergne et al, 2014; 2017).…”

Section: Discussionmentioning

confidence: 99%

Crumbs organizes the transport machinery by regulating apical levels of PI(4,5)P₂inDrosophila

Lattner

Leng

Knust

et al. 2019

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28An efficient vectorial intracellular transport machinery depends on a well-established apico-29 basal polarity and is a prerequisite for the function of secretory epithelia. Despite extensive 30 knowledge on individual trafficking pathways, little is known about the mechanisms 31 coordinating their temporal and spatial regulation. Here, we report that the polarity protein 32 Crumbs is essential for apical plasma membrane phospholipid-homeostasis and efficient 33 apical secretion. Through recruiting Heavy-Spectrin and MyosinV to the apical membrane, 34 Crumbs maintains the Rab6-, Rab11-and Rab30-dependent trafficking and regulates the lipid 35 phosphatases Pten and Ocrl. Crumbs knock-down results in increased apical levels of 36 PI(4,5)P2 and formation of a novel, Moesin-and PI(4,5)P2-enriched apical membrane sac 37 containing microvilli-like structures. Our results identify Crumbs as an essential hub required 38 to maintain the organization of the apical membrane and the physiological activity of the larval 39 salivary gland. 40 41 Epithelia can organize as layers or tubes, which form barriers and thus separate 43 internal biological compartments from the environment. Many epithelia are specialized for 44 absorption or secretion by performing selective and directional transport of nutrients, enzymes 45 and waste products, which is essential for metazoan life (Cereijido et al., 2004; Rodriguez-46 Boulan and Macara, 2014; Lemaitre and Miguel-Aliaga, 2013). To perform these functions, 47 epithelial cells are highly polarized: plasma membrane proteins and lipids are distributed 48 asymmetrically into an apical domain facing the environment or a lumen, and a basolateral 49 domain that contacts the neighboring cell and/or a basal lamina. In addition, polarity is 50 manifested by uneven distribution of organelles, asymmetric cytoskeleton organization and 51 directed trafficking (Rodriguez-Boulan and Macara, 2014; Knust and Bossinger, 2002; Eaton 52 and Martin-Belmonte, 2014). The latter is particularly obvious in secretory epithelia, for 53 example the salivary glands, which produce vast amounts of material that is secreted into the 54 gland lumen (Blasky et al., 2015; Iruela-Arispe and Beitel, 2013; Eaton and Martin-Belmonte, 55 2014; Chung et al., 2014; Miguel-Aliaga et al., 2018).56 Several evolutionarily conserved proteins regulate epithelial cell polarity. These include 57 members of the apical Crumbs-and PAR-complexes, and the basolateral Scrib-Dlg-Lgl 58 module (reviewed in (Flores-Benitez and Knust, 2016; Roman-Fernandez and Bryant, 2016)). 59The Crumbs (Crb) protein has a large extracellular domain (>2000 aa), and a small intracellular 60 domain (37 aa) (Tepass et al., 1990; Wodarz et al., 1993), which harbors two protein-protein 61 interaction motifs, a C-terminal PDZ (Postsynaptic density/Discs large/ZO-1)-domain binding 62 motif (PBM) and a juxtamembrane FERM (protein 4.1/ezrin/radixin/moesin)-domain binding 63 motif (FBM). The PBM is important for cell polarity and can bind Stardust (Sdt) and Par-6 (Li

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Stratum, a Homolog of the Human GEF Mss4, Partnered with Rab8, Controls the Basal Restriction of Basement Membrane Proteins in Epithelial Cells

Cited by 33 publications

References 31 publications

Clathrin adaptor AP-1 and Stratum act in parallel pathways to control Notch activation inDrosophilaSensory Organ Precursor Cells

Clathrin adaptor AP-1 and Stratum act in parallel pathways to control Notch activation inDrosophilaSensory Organ Precursor Cells

Oriented basement membrane fibrils provide a memory for F-actin planar polarization via the Dystrophin-Dystroglycan complex during tissue elongation

Crumbs organizes the transport machinery by regulating apical levels of PI(4,5)P₂inDrosophila

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Stratum, a Homolog of the Human GEF Mss4, Partnered with Rab8, Controls the Basal Restriction of Basement Membrane Proteins in Epithelial Cells

Cited by 33 publications

References 31 publications

Clathrin adaptor AP-1 and Stratum act in parallel pathways to control Notch activation inDrosophilaSensory Organ Precursor Cells

Clathrin adaptor AP-1 and Stratum act in parallel pathways to control Notch activation inDrosophilaSensory Organ Precursor Cells

Oriented basement membrane fibrils provide a memory for F-actin planar polarization via the Dystrophin-Dystroglycan complex during tissue elongation

Crumbs organizes the transport machinery by regulating apical levels of PI(4,5)P2inDrosophila

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Crumbs organizes the transport machinery by regulating apical levels of PI(4,5)P₂inDrosophila