p120-catenin binding masks an endocytic signal conserved in classical cadherins

Nanes, Benjamin A.; Chiasson-MacKenzie, Christine; Lowery, Anthony M.; Ishiyama, Noboru; Faúndez, Víctor; Ikura, Mitsuhiko; Vincent, Peter; Kowalczyk, Andrew P.

doi:10.1083/jcb.201205029

Cited by 174 publications

(222 citation statements)

References 51 publications

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“…Nevertheless, p120catenin depletion has a crucial impact on synaptogenesis [58] suggesting that, in these cells, p120catenin can control cadherin dynamics rather than cadherin expression. In fact, p120catenin may also contribute to cadherin turnover by masking another endocytic DEE signal conserved in the three most studied classical cadherins, E-cadherin, N-cadherin and VE-cadherin [54]. p120catenin also acts indirectly to modulate cadherin endocytosis.…”

Section: Membrane-associated P120catenin and The Regulation Of Adherementioning

confidence: 99%

p120catenin alteration in cancer and its role in tumour invasion

Péglion

Etienne-Manneville

2013

Phil. Trans. R. Soc. B

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Since its discovery in 1989 as a substrate of the Src oncogene, p120catenin has been revealed as an important player in cancer initiation and tumour dissemination. p120catenin regulates a wide range of cellular processes such as cell–cell adhesion, cell polarity and cell proliferation and plays a pivotal role in morphogenesis, inflammation and innate immunity. The pleiotropic effects of p120catenin rely on its interactions with numerous partners such as classical cadherins at the plasma membrane, Rho-GTPases and microtubules in the cytosol and transcriptional modulators in the nucleus. Alterations of p120catenin in cancer not only concern its expression level but also its intracellular localization and can lead to both pro-invasive and anti-invasive effects. This review focuses on the p120catenin-mediated pathways involved in cell migration and invasion and discusses the potential consequences of major cancer-related p120catenin alterations with respect to tumour spread.

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Section: Membrane-associated P120catenin and The Regulation Of Adherementioning

confidence: 99%

p120catenin alteration in cancer and its role in tumour invasion

Péglion

Etienne-Manneville

2013

Phil. Trans. R. Soc. B

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“…The latter pathway might affect immobile E-cad only or both subcomplexes. Evidence suggests that vertebrate cells also have p120-catenin-independent endocytic pathways, for example, a VE-cadherin mutant that cannot bind p120-catenin and lacked the endocytic motif is stabilised at the cell surface, but its surface levels are the same as wild type (Nanes et al, 2012).…”

Section: Two Pathways For E-cad Endocytosismentioning

confidence: 99%

“…The simplest way to explain this difference is that Drosophila E-cad lacks the endocytic motif. Two sequence motifs, LL and DEE, are crucial for internalisation of vertebrate cadherins (Miyashita and Ozawa, 2007;Nanes et al, 2012). The LL motif is absent from Drosophila E-cad, and is only found in vertebrate cadherins (Fig.…”

Section: Two Pathways For E-cad Endocytosismentioning

confidence: 99%

“…p120-catenin (also known as CTNND1 in vertebrates, and p120ctn in Drosophila) regulates cadherin endocytosis (Troyanovsky, 2009) by directly binding the cadherin intracellular domain and masking motifs necessary for endocytosis (Nanes et al, 2012). The p120-catenin family in vertebrates includes three additional proteins: δ-catenin (also known as CTNND2), ARVCF and p0071 (also known as PKP4) (Pieters et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

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Drosophila p120-catenin is crucial for endocytosis of the dynamic E-cadherin–Bazooka complex

Bulgakova¹,

Brown²

2016

Development

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The intracellular functions of classical cadherins are mediated through the direct binding of two catenins: β-catenin and p120-catenin (also known as CTNND1 in vertebrates, and p120ctn in Drosophila). Whereas β-catenin is crucial for cadherin function, the role of p120-catenin is less clear and appears to vary between organisms. We show here that p120-catenin has a conserved role in regulating the endocytosis of cadherins, but that its ancestral role might have been to promote endocytosis, followed by the acquisition of a new inhibitory role in vertebrates. In Drosophila, p120-catenin facilitates endocytosis of the dynamic E-cadherin-Bazooka subcomplex, which is followed by its recycling. The absence of p120-catenin stabilises this subcomplex at the membrane, reducing the ability of cells to exchange neighbours in embryos and expanding cell-cell contacts in imaginal discs.

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“…The interaction between VE-cadherin and p120-catenin/β-catenin is tightly regulated by (de-) phosphorylation and binding of p120-catenin to VE-cadherin inhibits the internalization of VE-cadherin. 4 Tyrosine phosphorylation of VE-cadherin reduces the interaction with p120-catenin and might therefore induce its internalization, resulting in disruption of AJs. Next to internalization, VE-cadherin is also regulated by cleavage 5 and through up or downregulation of its expression.…”

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confidence: 99%