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Adherens Junctions on the Move—Membrane Trafficking of E-Cadherin

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Adherens Junctions on the Move—Membrane Trafficking of E-Cadherin Downloaded from http://cshperspectives.cshlp.org/ on September 26, 2021 - Published by Cold Spring Harbor Laboratory Press Adherens Junctions on the Move—Membrane Trafficking of E-Cadherin Lena Bru¨ser1 and Sven Bogdan1,2 1Institut fu¨r Neurobiologie, Universita¨tMu¨nster, Badestraße 9, 48149 Mu¨nster, Germany 2Institut fu¨r Physiologie und Pathophysiologie, Abteilung Molekulare Zellphysiologie, Phillips-Universita¨t Marburg, Emil-Mannkopff-Straße 2, 35037 Marburg, Germany Correspondence: [email protected] Cadherin-based adherens junctions are conserved structuresthat mediate epithelial cell–cell adhesion in invertebrates andvertebrates. Despite their pivotal function in epithelial integrity, adherens junctions show a remarkable plasticity that is a prerequisite for tissue architecture and morphogenesis. Epithelial cadherin (E-cadherin) is continuously turned over and under- goes cycles of endocytosis, sorting and recycling back to the plasma membrane. Mammalian cell culture and genetically tractable model systems such as Drosophila have revealed con- served, but also distinct, mechanisms in the regulation of E-cadherin membrane trafficking. Here, we discuss our current knowledge about molecules and mechanisms controlling endocytosis, sorting and recycling of E-cadherin during junctional remodeling. he ability of epithelial cells to organize into Classical cadherins such as E-cadherin are Tmonolayered sheets is a prerequisite for single-pass membrane proteins with character- multicellularity, thereby providing tissue in- istic extracellular cadherin (EC) repeat do- tegrity, barrier function, and tissue polarity in mains that mediate trans-homophilic interac- metazoan organisms. Adherens junctions (AJs) tions between neighboring cells. While the are conserved key structures that mediate cell– numbers of ECs vary between different species, cell adhesion in invertebrates and vertebrates. In their intracellular domains are highly con- many polarized epithelial sheets, AJs form a served from flies to humans and form a com- continuous adhesive belt at the apical–lateral plex with catenins that link AJs to the actin interfaces of cell–cell contacts, the zonula ad- cytoskeleton. The juxtamembrane domain of herens. The structural and functional core com- the cadherin intracellular tail interacts with ponents of epithelial AJs are clusters of dimeric p120 catenin, whereas the carboxy-terminal E-cadherin, a calcium-dependent, homophilic part directly binds b-catenin, which, in turn, cell–cell adhesion receptor (Fig. 1). High-reso- binds a-catenin mediating a dynamic linkage lution microscopy analyses, however, recently to the actin cytoskeleton (Fig. 1) (Drees et al. revealed that E-cadherin clusters also accumu- 2005; Gates and Peifer 2005; Yamada et al. late throughout the lateral junctions below the 2005). This dynamic interaction between AJs zonula adherens (Wu et al. 2014; Yap et al. and the actin cytoskeleton is tightly linked to 2015). junctional maintenance, dynamics, and plastic- Editors: Carien M. Niessen and Alpha S. Yap Additional Perspectives on Cell–Cell Junctions available at www.cshperspectives.org Copyright # 2017 Cold Spring Harbor Laboratory Press; all rights reserved; doi: 10.1101/cshperspect.a029140 Cite this article as Cold Spring Harb Perspect Biol 2017;9:a029140 1 Downloaded from http://cshperspectives.cshlp.org/ on September 26, 2021 - Published by Cold Spring Harbor Laboratory Press L. Bru¨ser and S. Bogdan O-mannosylation N-glycosylation PM LL Y p120 p120 Src kinases SUMOylation β-Catenin β-Catenin AP-2 clathrin adaptor Uniquitin ligases (e.g., Hakai) α-Catenin α-Catenin Figure 1. The core E-cadherin/catenin complex at adherens junctions (AJs). The stability and turnover of the core E-cadherin/catenin complex is regulated by different molecules and posttranslational modifications, for further details see main text. ity in developing and differentiated tissues like Drosophila have led to the identification of (Michael and Yap 2013). conserved molecules and the underlying regu- The dual properties of stability and plastic- latory mechanisms driving cadherin trafficking ity of AJs were first observed in calcium chela- in a large variety of morphogenetic and devel- tion experiments (Kartenbeck et al. 1982). De- opmental processes. Here, we review our cur- pletion of extracellular calcium results in a rapid rent knowledge about the proteins and the disruption of cell–cell adhesion in cultured ep- mechanisms controlling endocytosis, sorting ithelial monolayers because of the endocytic in- and recycling of E-cadherin. ternalization of cadherins from AJs (Kartenbeck et al. 1982, 1991). The significance of cadherin E-CADHERIN IS CONSTANTLY internalization under physiological conditions INTERNALIZED FROM THE CELL SURFACE is now well established. Over the last three de- cades, numerous studies showed that junctional Dynamic changes in cell shape within tissues proteins such as E-cadherin are dynamically require a constant remodeling of cell junctions. turned over at the cell surface and this is funda- Initial metabolic labeling experiments in cul- mental for tissue remodeling during morpho- tured Madin–Darby canine kidney (MDCK) genesis and tissue homeostasis (Kowalczyk and epithelial cells showed a half-life of endogenous Nanes 2012; Takeichi 2014). Mammalian cell E-cadherin at the cell surface of 5–10 h culture studies combined with in vivo models (McCrea and Gumbiner 1991; Troxell et al. 2 Cite this article as Cold Spring Harb Perspect Biol 2017;9:a029140 Downloaded from http://cshperspectives.cshlp.org/ on September 26, 2021 - Published by Cold Spring Harbor Laboratory Press Membrane Trafficking of E-Cadherin 1999). Recent fluorescence recovery after photo- (Miranda et al. 2001; Miyashita and Ozawa bleaching (FRAP) and photoconversion exper- 2007a,b). iments in living epithelial layers of the Droso- The budding of clathrin-coated vesicles re- phila embryo confirmed a relatively slow quires the core endocytic machinery including biosynthetic turnover of E-cadherin clusters of the GTPases Dynamin and Rab5. Reduction of about 1 h in vivo (Cavey et al. 2008). Thus, the these core components results in an increase of comparatively slow transcriptional regulation of E-cadherin at the plasma membrane. Dynamin E-cadherin cannot account for all rapid changes is a large, multidomain GTPase that assembles in cell adhesion strength during fast cellular into helical structures along invaginating mem- movements and tissue remodeling. Instead, branes and drives the scission of endocytic ves- cadherins are constantly removed from the plas- icles through a cycle of oligomerization and ma membrane through endocytosis and recy- GTP hydrolysis (Fig. 2) (Schmid and Frolov cled back by exocytosis. Depending on the cel- 2011; Kirchhausen et al. 2014). Dynamin-medi- lular context, E-cadherin can be internalized ated endocytosis is required for E-cadherin re- through different endocytic pathways. Most distribution at mature AJs of MDCK and MCF7 studies analyzed clathrin-mediated endocytosis cells, but also plays an important role in AJ turn- of E-cadherin (Le et al. 1999; Palacios et al. 2002; over during Drosophila epithelial morphogene- Paterson et al. 2003). However, growth-factor- sis (Classen et al. 2005; Georgiou et al. 2008; induced non-clathrin-mediated pathways of Leibfried et al. 2008; de Beco et al. 2009; Levayer E-cadherin, including Rac1-dependent macro- et al. 2011). A key observation of the Drosophila pinocytosis, have been reported (Braga et al. in vivo studies is that E-cadherin endocytosis is 1997, 1999; Akhtar and Hotchin 2001; Lu locally enhanced along the planar axis or along et al. 2003; Bryant et al. 2007). the apico-basal axis of epithelial cells and that this local E-cadherin turnover has an instructive role in tissue morphogenesis. For example, po- LOCAL REMOVAL OF E-CADHERIN FROM larized endocytosis of E-cadherin is crucial for THE PLASMA MEMBRANE BY CLATHRIN- cell intercalations in the elongating Drosophila MEDIATED ENDOCYTOSIS embryo whereby epithelial cells change neigh- Unlike macropinocytosis, clathrin-mediated bors through the shrinkage of planar polarized endocytosis allows a spatially controlled inter- junctions along the dorsoventral axis. Blocking nalization. Since clathrin does not bind directly of clathrin-mediated endocytosis causes the loss to cargo receptors, selection of cargo relies on of E-cadherin planar polarization and a block of adaptor proteins that recognize internalization cell intercalations (Levayer et al. 2011). Similar motifs within the cytoplasmic region of trans- observations were made in Drosophila pupal ep- membrane receptors (Kelly and Owen 2011). E- ithelia (Classen et al. 2005; Georgiou et al. 2008; cadherin associates with several endocytic Leibfried et al. 2008; de Beco et al. 2009). Wing adaptors including AP-2, Dab-2, and Numb epithelial cells become hexagonally packed (Ling et al. 2007; Miyashita and Ozawa 2007b; through the shrinkage of individual AJ by po- Yang et al. 2007; Sato et al. 2011). A central larized E-cadherin turnover (Classen et al. 2005; adaptor in clathrin-mediated endocytosis is Warrington et al. 2013). Consistently, loss of AP-2, which forms a tetrameric complex that E-cadherin or dynamin function disrupts the directly binds clathrin and recruits several clas- planar polarized organization of the wing ses of receptors bearing an acidic dileucine in- epithelium (Classen et al. 2005; Fricke et al. ternalization signal in their cytoplasmic tail 2009). Polarized
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