Epithelial cells in tissues use their actin cytoskeletons to stick together, whereas unattached cells make active plasma membrane protrusions to migrate. In this issue, Wood et al. (2017. J. Cell Biol. https://doi.org/10.1083/jcb.201612006) show that the junction component α-catenin is critical in freely moving cells to promote adhesion and migration

Benjamin

Braga

Chinthalapudi

Drees

Edwards

Hansen

Klezovitch

Laura Machesky

Lien

Shewan

Vania M.M. Braga

Vasioukhin

Wood

English

Machesky, Laura

Braga, Vania M.M.

Enlighten: Publications

So far, yet so close: α-Catenin dimers help migrating cells get together

Enlighten

JCBJCB: SpotlightTHE JOURNAL OF CELL BIOLOGY3437The Rockefeller University Press J. Cell Biol. Vol. 216 No. 11 3437–3439https://doi.org/10.1083/jcb.201709056Actin-binding proteins regulate the assembly, organization, and contractility of actin filaments. Distinct sets of actin-binding proteins are found at cell–cell adhesions or cell–extracellular matrix attachments, with unique functions in organizing actin to scaffold, generate force, or signal. However, when cells change between free moving and tethered in a polarized epithelium, they need to repurpose their actin cytoskeletons. Thus, many actin-binding proteins change location and function. In truth, most actin-binding proteins have multiple functions, which may be in the insoluble cytoskeleton, cytoplasm, or nucleus. This helps the cell to coordinate environmental cues with the activi-ties or functions of each protein. It also raises interesting ques-tions about the mechanisms by which cells regulate the same proteins in different locations to perform specialized activities, depending on the context.The F-actin binding and bundling protein α-catenin is a prime example of a multifunctional protein with varied in-tracellular localization. It was originally identified as the in-direct link between the E-cadherin receptor cytoplasmic tail and the actin cytoskeleton. The α-catenin pool associated with E-cadherin complexes interacts with the cytoskeleton under force (Benjamin et al., 2010), which facilitates α-catenin bind-ing to other F-actin binding proteins to support cell–cell adhe-sion. However, α-catenin also localizes in the cytoplasm and in the nucleus. In the nucleus, α-catenin modulates transcriptional activity (Klezovitch and Vasioukhin, 2015), thereby controlling cell proliferation. In the cytoplasm, α-catenin may regulate ve-sicular trafficking via its interaction with dynamitin, a micro-tubule-binding protein (Lien et al., 2008). These functions of α-catenin in the cytosol are thought to be adhesion independent: the cell maintains different pools of α-catenin at distinct intra-cellular sites to be used in various processes. In this issue, Wood et al. shed light on a hidden facet of α-catenin: its localization at membrane protrusions and local modification of actin struc-tures underlying migration.By forcibly inducing the dimerization of α-catenin, the researchers found that it preferentially localizes at the plasma membrane, away from cadherin adhesive complexes at junc-tions. That α-catenin can dimerize is already known (Drees et al., 2005). However, how α-catenin dimers are formed, their precise function, or localization is uncharted territory. Using surface plasmon resonance, Wood et al. (2017) demonstrate a selective affinity of α-catenin homodimers for vesicles loaded with phospholipids, in particular phosphatidylinositol-3,4,5- trisphosphate (PIP3), whereas α-catenin monomers had no de-tectable binding (Fig. 1).α-Catenin mutants unable to interact with PIP3 maintained their ability to form homodimers, suggesting that phosphoinos-itide binding is not essential for interaction with membranes. However, PIP3 binding may also facilitate α-catenin homodimer formation via an increase in the local effective concentration of α-catenin at PIP3-rich sites on the plasma membrane. The authors speculate that, alternatively, phosphoinositide binding may induce a conformational change that favors dimerization and restricts free diffusion (Wood et al., 2017). This interpre-tation is consistent with the reduced ability of monomers to bind PIP3 and the fact that the dissociation constant of α-catenin dimers is higher than the concentration of cytosolic α-catenin (Drees et al., 2005). Alternatively, it is feasible that a lipid-bind-ing pocket in the dimeric structure forms through contributions of residues from the interface between the two α-catenin mono-mers. Although the authors could not confirm the latter because of the resolution of the α-catenin dimer crystal structures, a shared pocket between monomers has been previously shown to mediate phosphatidylinositol-4,5-bisphosphate (PIP2) binding in the close homologue vinculin (Chinthalapudi et al., 2014).Indeed, phospholipid association with cytoskeletal pro-teins is a known mechanism to modulate their function. For ex-ample, capping protein is thought to competitively bind to either the fast-growing end of actin filaments or PIP2 in the plasma membrane (Edwards et al., 2014). This regulation allows cells to rapidly trigger a burst of polymerization upon phosphoinosit-ide production, such as during platelet activation. Conversely, it also allows cells to rapidly clear actin off the plasma membrane after events such as phagocytic engulfment, when the actin coat is no longer needed and might interfere with trafficking.The findings by Wood et al. (2017) support the pro-posed contribution of phospholipids to organize and regulate Epithelial cells in tissues use their actin cytoskeletons to stick together, whereas unattached cells make active plasma membrane protrusions to migrate. In this issue, Wood et al. (2017. J. Cell Biol. https ://doi .org /10 .1083 /jcb .201612006) show that the junction component α-catenin is critical in freely moving cells to promote adhesion and migration.So far, yet so close: α-Catenin dimers help migrating cells get togetherLaura Machesky1 and Vania M.M. Braga21Cancer Research UK Beatson Institute, University of Glasgow, Glasgow, Scotland, UK 2National Heart and Lung Institute, Faculty of Medicine, Imperial College London, London, England, UK© 2017 Machesky and Braga This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http ://www .rupress .org /terms /). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https ://creativecommons .org /licenses /by -nc -sa /4 .0 /).Correspondence to Vania M.M. Braga: v.braga@imperial.ac.uk on November 14, 2017jcb.rupress.orgDownloaded from JCB • Volume 216 • NumBer 11 • 20173438cell architecture (Shewan et al., 2011). The results also add a new twist, by demonstrating the profound influence of PIP3- dependent localization of the α-catenin dimer on its cytoskeletal functions. Previous work has shown that α-catenin dimers can attenuate the barbed-end polymerization and actin-branching activity of Arp2/3 complexes in vitro (Drees et al., 2005) and protect filaments from severing (Hansen et al., 2013), favor-ing unbranched actin bundles. By forcibly inducing α-catenin dimerization, Wood et al. (2017) observed that dimers local-ize at nonjunctional membranes and strongly induce filopodia that are both longer and more abundant than in controls. These filopodia are thought to be key structures that initiate cell–cell contacts when epithelial cells approach each other. Thus, the plasma membrane recruitment via PIP3 and dimer formation of α-catenin may occur when cells are free of cell–cell contacts as a way of promoting cell–cell attachment and catalyzing epithelial tissue formation. This dual function for α-catenin thus nicely fits with a role in both promoting and stabilizing cell–cell adhesion.α-Catenin mutated to disable its interaction with PIP3 in-corporated into E-cadherin complexes and cosedimented with F-actin in vitro similar to wild type. Intriguingly, forcibly di-merizing this mutant weakened the mechanical strength of cell–cell junctions. Perhaps the filopodia that precede cell–cell junction formation, previously described as a zippering mech-anism (Vasioukhin et al., 2000), are important for correct as-sembly of junctions and stability. In polarized epithelial cells, it is possible that PIP3 localization at the basolateral domain (Shewan et al., 2011) potentially provides docking sites for α-catenin dimers at the cell–cell interface, independently of cadherin complexes. One can speculate that such events could modulate the properties of the actin cytoskeleton at junctions in a way to facilitate more stable adhesions (i.e., promoting lin-ear bundles of F-actin).In addition to the formation of extended filopodia displayed by α-catenin dimers, it is possible that α-catenin dimerization may impact the recruitment of signaling regulators to cell–cell contacts. Small GTPase regulators such as the exchange factor ECT2 or the GTPase-activating proteins (GAPs) MgcRacGAP and DLC1 require α-catenin for their localization at junctions (Braga, 2017). However, whether their recruitment or retention could be modulated by α-catenin homodimers has not yet been established. Alternatively, as most GTPase regulators contain a pleckstrin homology domain, it is also conceivable that an inter-action with lipids at the plasma membrane plays a role in their lo-calization, and α-catenin interaction could modulate their activity locally. Such regulation has been shown for the junction-resident proteins cingulin and Ajuba to inactivate the exchange factor GEF-H1 and the GAP CdGAP, respectively (Braga, 2017).Overall, the newly described dimerization and switch in function of α-catenin between the plasma membrane and cell–cell contacts suggest an important role in the establish-ment of new cell–cell contacts as well as maintenance of ex-isting ones, which could contribute to tissue development and remodeling. It makes sense that actin-binding proteins would have different localizations and functions in cells when they are either freely migrating before tissue establishment or coming together to form multicellular tissues. It will be interesting to test whether α-catenin dimers are also formed when tissues are injured and participate in filopodia formation in the context of wound healing and repair.AcknowledgmentsThe authors declare no competing financial interests.ReferencesBenjamin, J.M., A.V.  Kwiatkowski, C.  Yang, F.  Korobova, S.  Pokutta, T. Svitkina, W.I. Weis, and W.J. Nelson. 2010. αE-catenin regulates actin dynamics independently of cadherin-mediated cell–cell adhesion. J. Cell Biol. 189:339–352. https ://doi .org /10 .1083 /jcb .200910041Braga, V.  2017. Signaling by Small GTPases at Cell-Cell junctions: Protein Interactions Building Control and Networks. Cold Spring Harb. Perspect. Biol.:a028746. https ://doi .org /10 .1101 /cshperspect .a028746Chinthalapudi, K., E.S.  Rangarajan, D.N.  Patil, E.M.  George, D.T.  Brown, and T.  Izard. 2014. Lipid binding promotes oligomerization and focal adhesion activity of vinculin. J. Cell Biol. 207:643–656. https ://doi .org /10 .1083 /jcb .201404128Drees, F., S. Pokutta, S. Yamada, W.J. Nelson, and W.I. Weis. 2005. α-catenin is a molecular switch that binds E-cadherin-β-catenin and regulates actin-Figure 1. The dimeric form of α-catenin interacts preferentially with PIP3 at the membrane of single cells and promotes the formation of long, extended filopodia that may establish attachment with neighboring cells. Monomeric α-catenin is the form that interacts with β-catenin in cadherin complexes at ad-hesion sites. Forcible dimerization of α-catenin mutants that do not bind PIP3 prevents filopodia formation and promotes faster wound closure of epithelial sheets. Strikingly, expression of these PIP3-binding defective mutants also interferes with the stability of cadherin-based adhesions. on November 14, 2017jcb.rupress.orgDownloaded from Catenin dimers help migrating cells get together • machesky and Braga 3439filament assembly. Cell. 123:903–915. https ://doi .org /10 .1016 /j .cell .2005 .09 .021Edwards, M., A. Zwolak, D.A. Schafer, D. Sept, R. Dominguez, and J.A. Cooper. 2014. Capping protein regulators fine-tune actin assembly dynamics. Nat. Rev. Mol. Cell Biol. 15:677–689. https ://doi .org /10 .1038 /nrm3869Hansen, S.D., A.V. Kwiatkowski, C.Y. Ouyang, H. Liu, S. Pokutta, S.C. Watkins, N. Volkmann, D. Hanein, W.I. Weis, R.D. Mullins, and W.J. Nelson. 2013. αE-catenin actin-binding domain alters actin filament conformation and regulates binding of nucleation and disassembly factors. Mol. Biol. Cell. 24:3710–3720. https ://doi .org /10 .1091 /mbc .E13 -07 -0388Klezovitch, O., and V. Vasioukhin. 2015. Cadherin signaling: keeping cells in touch. F1000 Res. 4(F1000 Faculty Rev):550. https ://doi .org /10 .12688 /f1000research .6445 .1Lien, W.H., V.I.  Gelfand, and V.  Vasioukhin. 2008. α–E-catenin binds to dynamitin and regulates dynactin-mediated intracellular traffic. J.  Cell Biol. 183:989–997. https ://doi .org /10 .1083 /jcb .200805041Shewan, A., D.J.  Eastburn, and K.  Mostov. 2011. Phosphoinositides in cell architecture. Cold Spring Harb. Perspect. Biol. 3:a004796. https ://doi .org /10 .1101 /cshperspect .a004796Vasioukhin, V., C.  Bauer, M.  Yin, and E.  Fuchs. 2000. Directed actin polymerization is the driving force for epithelial cell–cell adhesion. Cell. 100:209–219. https ://doi .org /10 .1016 /S0092 -8674(00)81559 -7Wood, M.N., N. Ishiyama, I. Singaram, C.M. Chung, A.S. Flozak, A. Yemelyanov, M.  Ikura, W. Cho, and C.J. Gottardi. 2017. α-Catenin homodimers are recruited to phosphoinositide-activated membranes to promote adhesion. J. Cell Biol. https ://doi .org /10 .1083 /jcb .201612006 on November 14, 2017jcb.rupress.orgDownloaded from 

Epithelial cells in tissues use their actin cytoskeletons to stick together, whereas unattached cells make active plasma membrane protrusions to migrate. In this issue, Wood et al. (2017. J. Cell Biol. https://doi.org/10.1083/jcb.201612006) show that the junction component α-catenin is critical in freely moving cells to promote adhesion and migration.</jats:p

Crossref

JCBJCB: SpotlightTHE JOURNAL OF CELL BIOLOGY3437The Rockefeller University Press J. Cell Biol. Vol. 216 No. 11 3437–3439https://doi.org/10.1083/jcb.201709056Actin-binding proteins regulate the assembly, organization, and contractility of actin filaments. Distinct sets of actin-binding proteins are found at cell–cell adhesions or cell–extracellular matrix attachments, with unique functions in organizing actin to scaffold, generate force, or signal. However, when cells change between free moving and tethered in a polarized epithelium, they need to repurpose their actin cytoskeletons. Thus, many actin-binding proteins change location and function. In truth, most actin-binding proteins have multiple functions, which may be in the insoluble cytoskeleton, cytoplasm, or nucleus. This helps the cell to coordinate environmental cues with the activi-ties or functions of each protein. It also raises interesting ques-tions about the mechanisms by which cells regulate the same proteins in different locations to perform specialized activities, depending on the context.The F-actin binding and bundling protein α-catenin is a prime example of a multifunctional protein with varied in-tracellular localization. It was originally identified as the in-direct link between the E-cadherin receptor cytoplasmic tail and the actin cytoskeleton. The α-catenin pool associated with E-cadherin complexes interacts with the cytoskeleton under force (Benjamin et al., 2010), which facilitates α-catenin bind-ing to other F-actin binding proteins to support cell–cell adhe-sion. However, α-catenin also localizes in the cytoplasm and in the nucleus. In the nucleus, α-catenin modulates transcriptional activity (Klezovitch and Vasioukhin, 2015), thereby controlling cell proliferation. In the cytoplasm, α-catenin may regulate ve-sicular trafficking via its interaction with dynamitin, a micro-tubule-binding protein (Lien et al., 2008). These functions of α-catenin in the cytosol are thought to be adhesion independent: the cell maintains different pools of α-catenin at distinct intra-cellular sites to be used in various processes. In this issue, Wood et al. shed light on a hidden facet of α-catenin: its localization at membrane protrusions and local modification of actin struc-tures underlying migration.By forcibly inducing the dimerization of α-catenin, the researchers found that it preferentially localizes at the plasma membrane, away from cadherin adhesive complexes at junc-tions. That α-catenin can dimerize is already known (Drees et al., 2005). However, how α-catenin dimers are formed, their precise function, or localization is uncharted territory. Using surface plasmon resonance, Wood et al. (2017) demonstrate a selective affinity of α-catenin homodimers for vesicles loaded with phospholipids, in particular phosphatidylinositol-3,4,5- trisphosphate (PIP3), whereas α-catenin monomers had no de-tectable binding (Fig. 1).α-Catenin mutants unable to interact with PIP3 maintained their ability to form homodimers, suggesting that phosphoinos-itide binding is not essential for interaction with membranes. However, PIP3 binding may also facilitate α-catenin homodimer formation via an increase in the local effective concentration of α-catenin at PIP3-rich sites on the plasma membrane. The authors speculate that, alternatively, phosphoinositide binding may induce a conformational change that favors dimerization and restricts free diffusion (Wood et al., 2017). This interpre-tation is consistent with the reduced ability of monomers to bind PIP3 and the fact that the dissociation constant of α-catenin dimers is higher than the concentration of cytosolic α-catenin (Drees et al., 2005). Alternatively, it is feasible that a lipid-bind-ing pocket in the dimeric structure forms through contributions of residues from the interface between the two α-catenin mono-mers. Although the authors could not confirm the latter because of the resolution of the α-catenin dimer crystal structures, a shared pocket between monomers has been previously shown to mediate phosphatidylinositol-4,5-bisphosphate (PIP2) binding in the close homologue vinculin (Chinthalapudi et al., 2014).Indeed, phospholipid association with cytoskeletal pro-teins is a known mechanism to modulate their function. For ex-ample, capping protein is thought to competitively bind to either the fast-growing end of actin filaments or PIP2 in the plasma membrane (Edwards et al., 2014). This regulation allows cells to rapidly trigger a burst of polymerization upon phosphoinosit-ide production, such as during platelet activation. Conversely, it also allows cells to rapidly clear actin off the plasma membrane after events such as phagocytic engulfment, when the actin coat is no longer needed and might interfere with trafficking.The findings by Wood et al. (2017) support the pro-posed contribution of phospholipids to organize and regulate Epithelial cells in tissues use their actin cytoskeletons to stick together, whereas unattached cells make active plasma membrane protrusions to migrate. In this issue, Wood et al. (2017. J. Cell Biol. https ://doi .org /10 .1083 /jcb .201612006) show that the junction component α-catenin is critical in freely moving cells to promote adhesion and migration.So far, yet so close: α-Catenin dimers help migrating cells get togetherLaura Machesky1 and Vania M.M. Braga21Cancer Research UK Beatson Institute, University of Glasgow, Glasgow, Scotland, UK 2National Heart and Lung Institute, Faculty of Medicine, Imperial College London, London, England, UK© 2017 Machesky and Braga This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http ://www .rupress .org /terms /). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https ://creativecommons .org /licenses /by -nc -sa /4 .0 /).Correspondence to Vania M.M. Braga: v.braga@imperial.ac.uk on January 2, 2018jcb.rupress.orgDownloaded from JCB • Volume 216 • NumBer 11 • 20173438cell architecture (Shewan et al., 2011). The results also add a new twist, by demonstrating the profound influence of PIP3- dependent localization of the α-catenin dimer on its cytoskeletal functions. Previous work has shown that α-catenin dimers can attenuate the barbed-end polymerization and actin-branching activity of Arp2/3 complexes in vitro (Drees et al., 2005) and protect filaments from severing (Hansen et al., 2013), favor-ing unbranched actin bundles. By forcibly inducing α-catenin dimerization, Wood et al. (2017) observed that dimers local-ize at nonjunctional membranes and strongly induce filopodia that are both longer and more abundant than in controls. These filopodia are thought to be key structures that initiate cell–cell contacts when epithelial cells approach each other. Thus, the plasma membrane recruitment via PIP3 and dimer formation of α-catenin may occur when cells are free of cell–cell contacts as a way of promoting cell–cell attachment and catalyzing epithelial tissue formation. This dual function for α-catenin thus nicely fits with a role in both promoting and stabilizing cell–cell adhesion.α-Catenin mutated to disable its interaction with PIP3 in-corporated into E-cadherin complexes and cosedimented with F-actin in vitro similar to wild type. Intriguingly, forcibly di-merizing this mutant weakened the mechanical strength of cell–cell junctions. Perhaps the filopodia that precede cell–cell junction formation, previously described as a zippering mech-anism (Vasioukhin et al., 2000), are important for correct as-sembly of junctions and stability. In polarized epithelial cells, it is possible that PIP3 localization at the basolateral domain (Shewan et al., 2011) potentially provides docking sites for α-catenin dimers at the cell–cell interface, independently of cadherin complexes. One can speculate that such events could modulate the properties of the actin cytoskeleton at junctions in a way to facilitate more stable adhesions (i.e., promoting lin-ear bundles of F-actin).In addition to the formation of extended filopodia displayed by α-catenin dimers, it is possible that α-catenin dimerization may impact the recruitment of signaling regulators to cell–cell contacts. Small GTPase regulators such as the exchange factor ECT2 or the GTPase-activating proteins (GAPs) MgcRacGAP and DLC1 require α-catenin for their localization at junctions (Braga, 2017). However, whether their recruitment or retention could be modulated by α-catenin homodimers has not yet been established. Alternatively, as most GTPase regulators contain a pleckstrin homology domain, it is also conceivable that an inter-action with lipids at the plasma membrane plays a role in their lo-calization, and α-catenin interaction could modulate their activity locally. Such regulation has been shown for the junction-resident proteins cingulin and Ajuba to inactivate the exchange factor GEF-H1 and the GAP CdGAP, respectively (Braga, 2017).Overall, the newly described dimerization and switch in function of α-catenin between the plasma membrane and cell–cell contacts suggest an important role in the establish-ment of new cell–cell contacts as well as maintenance of ex-isting ones, which could contribute to tissue development and remodeling. It makes sense that actin-binding proteins would have different localizations and functions in cells when they are either freely migrating before tissue establishment or coming together to form multicellular tissues. It will be interesting to test whether α-catenin dimers are also formed when tissues are injured and participate in filopodia formation in the context of wound healing and repair.AcknowledgmentsThe authors declare no competing financial interests.ReferencesBenjamin, J.M., A.V.  Kwiatkowski, C.  Yang, F.  Korobova, S.  Pokutta, T. Svitkina, W.I. Weis, and W.J. Nelson. 2010. αE-catenin regulates actin dynamics independently of cadherin-mediated cell–cell adhesion. J. Cell Biol. 189:339–352. https ://doi .org /10 .1083 /jcb .200910041Braga, V.  2017. Signaling by Small GTPases at Cell-Cell junctions: Protein Interactions Building Control and Networks. Cold Spring Harb. Perspect. Biol.:a028746. https ://doi .org /10 .1101 /cshperspect .a028746Chinthalapudi, K., E.S.  Rangarajan, D.N.  Patil, E.M.  George, D.T.  Brown, and T.  Izard. 2014. Lipid binding promotes oligomerization and focal adhesion activity of vinculin. J. Cell Biol. 207:643–656. https ://doi .org /10 .1083 /jcb .201404128Drees, F., S. Pokutta, S. Yamada, W.J. Nelson, and W.I. Weis. 2005. α-catenin is a molecular switch that binds E-cadherin-β-catenin and regulates actin-Figure 1. The dimeric form of α-catenin interacts preferentially with PIP3 at the membrane of single cells and promotes the formation of long, extended filopodia that may establish attachment with neighboring cells. Monomeric α-catenin is the form that interacts with β-catenin in cadherin complexes at ad-hesion sites. Forcible dimerization of α-catenin mutants that do not bind PIP3 prevents filopodia formation and promotes faster wound closure of epithelial sheets. Strikingly, expression of these PIP3-binding defective mutants also interferes with the stability of cadherin-based adhesions. on January 2, 2018jcb.rupress.orgDownloaded from Catenin dimers help migrating cells get together • machesky and Braga 3439filament assembly. Cell. 123:903–915. https ://doi .org /10 .1016 /j .cell .2005 .09 .021Edwards, M., A. Zwolak, D.A. Schafer, D. Sept, R. Dominguez, and J.A. Cooper. 2014. Capping protein regulators fine-tune actin assembly dynamics. Nat. Rev. Mol. Cell Biol. 15:677–689. https ://doi .org /10 .1038 /nrm3869Hansen, S.D., A.V. Kwiatkowski, C.Y. Ouyang, H. Liu, S. Pokutta, S.C. Watkins, N. Volkmann, D. Hanein, W.I. Weis, R.D. Mullins, and W.J. Nelson. 2013. αE-catenin actin-binding domain alters actin filament conformation and regulates binding of nucleation and disassembly factors. Mol. Biol. Cell. 24:3710–3720. https ://doi .org /10 .1091 /mbc .E13 -07 -0388Klezovitch, O., and V. Vasioukhin. 2015. Cadherin signaling: keeping cells in touch. F1000 Res. 4(F1000 Faculty Rev):550. https ://doi .org /10 .12688 /f1000research .6445 .1Lien, W.H., V.I.  Gelfand, and V.  Vasioukhin. 2008. α–E-catenin binds to dynamitin and regulates dynactin-mediated intracellular traffic. J.  Cell Biol. 183:989–997. https ://doi .org /10 .1083 /jcb .200805041Shewan, A., D.J.  Eastburn, and K.  Mostov. 2011. Phosphoinositides in cell architecture. Cold Spring Harb. Perspect. Biol. 3:a004796. https ://doi .org /10 .1101 /cshperspect .a004796Vasioukhin, V., C.  Bauer, M.  Yin, and E.  Fuchs. 2000. Directed actin polymerization is the driving force for epithelial cell–cell adhesion. Cell. 100:209–219. https ://doi .org /10 .1016 /S0092 -8674(00)81559 -7Wood, M.N., N. Ishiyama, I. Singaram, C.M. Chung, A.S. Flozak, A. Yemelyanov, M.  Ikura, W. Cho, and C.J. Gottardi. 2017. α-Catenin homodimers are recruited to phosphoinositide-activated membranes to promote adhesion. J. Cell Biol. https ://doi .org /10 .1083 /jcb .201612006 on January 2, 2018jcb.rupress.orgDownloaded from 

So far, yet so close: α-Catenin dimers help migrating cells get together

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