Proteomic analysis of adaptor protein 1A coats selectively assembled on liposomes

Baust, Thorsten; Czupalla, Cornelia; Krause, Eberhard; Bourel-Bonnet, Line; Hoflack, Bernard

doi:10.1073/pnas.0511062103

Cited by 51 publications

(78 citation statements)

References 53 publications

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“…Alternatively, AP-1 could also directly contribute to actin organisation: a proteomic analysis showed that several actin nucleators were found on AP-1-enriched liposomes (Baust et al, 2006). We therefore cannot exclude that the loss of AP-1 could also have a direct impact on actin organisation through these actin cofactors, independently of E-cad.…”

Section: Discussionmentioning

confidence: 97%

Control of E-cadherin apical localisation and morphogenesis by a SOAP-1/AP-1/clathrin pathway in C. elegans epidermal cells

et al. 2015

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E-cadherin (E-cad) is the main component of epithelial junctions in multicellular organisms, where it is essential for cell-cell adhesion. The localisation of E-cad is often strongly polarised in the apicobasal axis. However, the mechanisms required for its polarised distribution are still largely unknown. We performed a systematic RNAi screen in vivo to identify genes required for the strict E-cad apical localisation in C. elegans epithelial epidermal cells. We found that the loss of clathrin, its adaptor AP-1 and the AP-1 interactor SOAP-1 induced a basolateral localisation of E-cad without affecting the apico-basal diffusion barrier. We further found that SOAP-1 controls AP-1 localisation, and that AP-1 is required for clathrin recruitment. Finally, we also show that AP-1 controls Ecad apical delivery and actin organisation during embryonic elongation, the final morphogenetic step of embryogenesis. We therefore propose that a molecular pathway, containing SOAP-1, AP-1 and clathrin, controls the apical delivery of E-cad and morphogenesis.

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Section: Discussionmentioning

confidence: 97%

Control of E-cadherin apical localisation and morphogenesis by a SOAP-1/AP-1/clathrin pathway in C. elegans epidermal cells

et al. 2015

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“…Given that the amino acid sequence of the intracellular tails of all Crb proteins are highly conserved from Drosophila to mammals (Fig. 1A), we incubated mouse Crb2 (mCrb2) tail-coupled liposomes with an adaptor mixture isolated from pig brain (Baust et al, 2006;Crottet et al, 2002). This mixture was highly enriched in constituents of the AP-2 complex (Fig.…”

Section: α-Ada Associates With Crbmentioning

confidence: 99%

AP-2-complex-mediated endocytosis of Drosophila Crumbs regulates polarity by antagonizing Stardust

Lin

Currinn

Pocha

et al. 2015

Journal of Cell Science

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Maintenance of epithelial polarity depends on the correct localization and levels of polarity determinants. The evolutionarily conserved transmembrane protein Crumbs is crucial for the size and identity of the apical membrane, yet little is known about the molecular mechanisms controlling the amount of Crumbs at the surface. Here, we show that Crumbs levels on the apical membrane depend on a well-balanced state of endocytosis and stabilization. The adaptor protein 2 (AP-2) complex binds to a motif in the cytoplasmic tail of Crumbs that overlaps with the binding site of Stardust, a protein known to stabilize Crumbs on the surface. Preventing endocytosis by mutation of AP-2 causes expansion of the Crumbspositive plasma membrane domain and polarity defects, which can be partially rescued by removing one copy of crumbs. Strikingly, knocking down both AP-2 and Stardust leads to the retention of Crumbs on the membrane. This study provides evidence for a molecular mechanism, based on stabilization and endocytosis, to adjust surface levels of Crumbs, which are essential for maintaining epithelial polarity.

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“…Interestingly, CDC-42 has been found on AP-1A coated liposomes (Baust et al, 2006), which raises the possibility of a physical interaction between CDC-42 and AP-1, which could be required to prevent or limit CDC-42 basolateral targeting and promote its apical sorting. We propose that by controlling the sorting of both apical and basolateral proteins, including CDC-42 and PAR-6 AP-1 is a crucial factor in apicobasal polarity maintenance, whereas the interactions between AP-1, clathrin and GSL remain to be elucidated.…”

Section: Research Articlementioning

confidence: 99%

AP-1 is required for the maintenance of apico-basal polarity in theC. elegansintestine

et al. 2012

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SUMMARYEpithelial tubes perform functions that are essential for the survival of multicellular organisms. Understanding how their polarised features are maintained is therefore crucial. By analysing the function of the clathrin adaptor AP-1 in the C. elegans intestine, we found that AP-1 is required for epithelial polarity maintenance. Depletion of AP-1 subunits does not affect epithelial polarity establishment or the formation of the intestinal lumen. However, the loss of AP-1 affects the polarised distribution of both apical and basolateral transmembrane proteins. Moreover, it triggers de novo formation of ectopic apical lumens between intestinal cells along the lateral membranes later during embryogenesis. We also found that AP-1 is specifically required for the apical localisation of the small GTPase CDC-42 and the polarity determinant PAR-6. Our results demonstrate that AP-1 controls an apical trafficking pathway required for the maintenance of epithelial polarity in vivo in a tubular epithelium.

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Proteomic analysis of adaptor protein 1A coats selectively assembled on liposomes

Cited by 51 publications

References 53 publications

Control of E-cadherin apical localisation and morphogenesis by a SOAP-1/AP-1/clathrin pathway in C. elegans epidermal cells

Control of E-cadherin apical localisation and morphogenesis by a SOAP-1/AP-1/clathrin pathway in C. elegans epidermal cells

AP-2-complex-mediated endocytosis of Drosophila Crumbs regulates polarity by antagonizing Stardust

AP-1 is required for the maintenance of apico-basal polarity in theC. elegansintestine

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