The F-box protein Slmb restricts the activity of aPKC to polarize epithelial cells

Skwarek, Lara C.; Windler, Sarah L.; Vreede, Geert de; Rogers, Gerald S.; Bilder, David

doi:10.1242/dev.109694

Cited by 9 publications

(9 citation statements)

References 39 publications

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“…Par-1 plays the dominant role, whereas Lgl plays a smaller role that can be enhanced by overexpression (Morais- de-Sá et al, 2014;Tian and Deng, 2008). While Drosophila lack a homologue of PAR-2, an E3 ubiquitin ligase called Slmb may play an analogous role in the sense that Slmb is required for posterior accumulation of Par-1 and the establishment of oocyte polarity, and loss of Slmb can be rescued by overexpressing Lgl (Morais- de-Sá et al, 2014;Skwarek et al, 2014). Whether posterior inhibition of Cdc-42 activity is also involved remains unclear.…”

Section: Par Asymmetries In Drosophila Oocytesmentioning

confidence: 99%

The PAR proteins: from molecular circuits to dynamic self-stabilizing cell polarity

2017

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PAR proteins constitute a highly conserved network of scaffolding proteins, adaptors and enzymes that form and stabilize cortical asymmetries in response to diverse inputs. They function throughout development and across the metazoa to regulate cell polarity. In recent years, traditional approaches to identifying and characterizing molecular players and interactions in the PAR network have begun to merge with biophysical, theoretical and computational efforts to understand the network as a pattern-forming biochemical circuit. Here, we summarize recent progress in the field, focusing on recent studies that have characterized the core molecular circuitry, circuit design and spatiotemporal dynamics. We also consider some of the ways in which the PAR network has evolved to polarize cells in different contexts and in response to different cues and functional constraints.

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Section: Par Asymmetries In Drosophila Oocytesmentioning

confidence: 99%

The PAR proteins: from molecular circuits to dynamic self-stabilizing cell polarity

2017

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“…Slmb is an adaptor of the SCF E3 ligase complex that restricts the apical domain of Drosophila melanogaster imaginal epithelia by limiting the activity of aPKC in a seemingly degradation‐independent manner (Skwarek et al, ), and also controls the polarity in Drosophila oocyte and follicular epithelium through targeting the Par6/aPKC complex for degradation (Morais‐de‐Sa et al, ). In addition to directly mediating ubiquitination of Par components, E3 ligases also act on downstream effectors to regulate ABP during epithelial morphogenesis.…”

Section: Ubiquitination In Cellular Events Of Epithelial Morphogenesismentioning

confidence: 99%

Degradation for better survival? Role of ubiquitination in epithelial morphogenesis

Cheng

Zheng

et al. 2018

Biological Reviews

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As a prevalent post-translational modification, ubiquitination is essential for many developmental processes. Once covalently attached to the small and conserved polypeptide ubiquitin (Ub), a substrate protein can be directed to perform specific biological functions via its Ub-modified form. Three sequential catalytic reactions contribute to this process, among which E3 ligases serve to identify target substrates and promote the activated Ub to conjugate to substrate proteins. Ubiquitination has great plasticity, with diverse numbers, topologies and modifications of Ub chains conjugated at different substrate residues adding a layer of complexity that facilitates a huge range of cellular functions. Herein, we highlight key advances in the understanding of ubiquitination in epithelial morphogenesis, with an emphasis on the latest insights into its roles in cellular events involved in polarized epithelial tissue, including cell adhesion, asymmetric localization of polarity determinants and cytoskeletal organization. In addition, the physiological roles of ubiquitination are discussed for typical examples of epithelial morphogenesis, such as lung branching, vascular development and synaptic formation and plasticity. Our increased understanding of ubiquitination in epithelial morphogenesis may provide novel insights into the molecular mechanisms underlying epithelial regeneration and maintenance.

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“…Other sorts of cross‐regulatory interactions between the apical and basal Par proteins also contribute to the polarization process. For example aPKC activity is limited to the apical domain through the action Supernumerary Limbs (Slmb), a substrate adaptor for an E3 ubiquitin ligase, while from the basolateral domain .…”

Section: Establishing and Maintaining Polarity Requires Feedback Mechmentioning

confidence: 99%

Establishing and maintaining cell polarity with mRNA localization in Drosophila

et al. 2016

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How cell polarity is established and maintained is an important question in diverse biological contexts. Molecular mechanisms used to localize polarity proteins to distinct domains are likely context-dependent and provide a feedback loop in order to maintain polarity. One such mechanism is the localized translation of mRNAs encoding polarity proteins, which will be the focus of this review and may play a more important role in the establishment and maintenance of polarity than is currently known. Localized translation of mRNAs encoding polarity proteins can be used to establish polarity in response to an external signal, and to maintain polarity by local production of polarity determinants. The importance of this mechanism is illustrated by recent findings, including orb2-dependent localized translation of aPKC mRNA at the apical end of elongating spermatid tails in the Drosophila testis, and the apical localization of stardust A mRNA in Drosophila follicle and embryonic epithelia.

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The F-box protein Slmb restricts the activity of aPKC to polarize epithelial cells

Cited by 9 publications

References 39 publications

The PAR proteins: from molecular circuits to dynamic self-stabilizing cell polarity

The PAR proteins: from molecular circuits to dynamic self-stabilizing cell polarity

Degradation for better survival? Role of ubiquitination in epithelial morphogenesis

Establishing and maintaining cell polarity with mRNA localization in Drosophila

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