p120 Catenin Regulates Dendritic Spine and Synapse Development through Rho-Family GTPases and Cadherins

Elia, Lisa P.; Yamamoto, Myrtle; Zang, Keling; Reichardt, Louis F.

doi:10.1016/j.neuron.2006.05.018

Cited by 192 publications

(237 citation statements)

References 70 publications

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“…More recently, conflicting in vitro and in vivo observations suggested that the role of p120catenin in the regulation of Rho-GTPases may be tissue-and context-dependent [106]. In vivo data in the mouse epidermis [14] and forebrain [58] confirmed the role of p120catenin in RhoA inhibition. This regulatory process can occur in the cytosol through a direct interaction between RhoA and the amino-terminal domain and a central polybasic region of p120catenin [107,108] (figure 2).…”

Section: (B) Cytosolic P120catenin Interacts With and Modulates Rho-gmentioning

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: (B) Cytosolic P120catenin Interacts With and Modulates Rho-gmentioning

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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“…To directly study roles for p120 in vivo, conditional p120 KO mouse models have been generated by our group (32) and by the Reichardt laboratory (33). p120 KO in the intestine has not been described.…”

Section: Introductionmentioning

confidence: 99%

p120-catenin is essential for maintenance of barrier function and intestinal homeostasis in mice

Smalley-Freed¹,

Ефимов²,

Burnett³

et al. 2010

J. Clin. Invest.

123

152

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Epithelial-cadherin (E-cadherin) is a master organizer of the epithelial phenotype. Its function is regulated in part by p120-catenin (referred to herein as p120), a cytoplasmic binding partner that directly regulates cadherin stability. As it has been suggested that cadherins have a role in inflammatory bowel disease (IBD), we sought to investigate this further by assessing the effect of p120 deficiency in mouse small intestine and colon. p120 conditional KO mice were superficially normal at birth but declined rapidly and died within 21 days. Cellcell adhesion defects and inflammation led to progressive mucosal erosion and terminal bleeding, similar to what is observed in a dominant-negative cadherin mouse model of IBD. Additionally, selective loss of adherens junctions and accumulation of atypical COX-2-expressing neutrophils in p120-null areas of the colon were observed. To elucidate the mechanism, direct effects of p120 deficiency were assessed in vitro in a polarizing colon cancer cell line. Notably, transepithelial electrical resistance was dramatically reduced, neutrophil binding was increased 30 fold, and levels of COX-2, an enzyme associated with IBD, were markedly increased in neutrophils. Our data suggest that p120 loss disrupts the neonatal intestinal barrier and amplifies neutrophil engagement and that these changes lead to catastrophic inflammation during colonization of the neonatal gut with bacteria and other luminal antigens. Thus, we conclude that p120 has an essential role in barrier function and epithelial homeostasis and survival in the intestine.

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“…In addition to its important postsynaptic roles (4,(16)(17)(18), N-cadherin has been suggested to be involved in the formation of presynaptic vesicle clusters (4,16,19,20). However, these findings could not yet be confirmed in N-cadherin knockout neurons (21,22), and expression of N-cadherin in nonneuronal cells does not induce clustering of synaptic vesicles in contacting axons (3,9).…”

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confidence: 99%

Essential cooperation of N-cadherin and neuroligin-1 in the transsynaptic control of vesicle accumulation

Stan¹,

Pielarski²,

Brigadski

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

116

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Cell adhesion molecules are key players in transsynaptic communication, precisely coordinating presynaptic differentiation with postsynaptic specialization. At glutamatergic synapses, their retrograde signaling has been proposed to control presynaptic vesicle clustering at active zones. However, how the different types of cell adhesion molecules act together during this decisive step of synapse maturation is largely unexplored. Using a knockout approach, we show that two synaptic adhesion systems, N-cadherin and neuroligin-1, cooperate to control vesicle clustering at nascent synapses. Live cell imaging and fluorescence recovery after photobleaching experiments at individual synaptic boutons revealed a strong impairment of vesicle accumulation in the absence of N-cadherin, whereas the formation of active zones was largely unaffected. Strikingly, also the clustering of synaptic vesicles triggered by neuroligin-1 overexpression required the presence of N-cadherin in cultured neurons. Mechanistically, we found that N-cadherin acts by postsynaptically accumulating neuroligin-1 and activating its function via the scaffolding molecule S-SCAM, leading, in turn, to presynaptic vesicle clustering. A similar cooperation of N-cadherin and neuroligin-1 was observed in immature CA3 pyramidal neurons in an organotypic hippocampal network. Moreover, at mature synapses, N-cadherin was required for the increase in release probability and miniature EPSC frequency induced by expressed neuroligin-1. This cooperation of two cell adhesion systems provides a mechanism for coupling bidirectional synapse maturation mediated by neuroligin-1 to cell type recognition processes mediated by classical cadherins.synapse maturation | synaptic adhesion molecules | vesicle clustering

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p120 Catenin Regulates Dendritic Spine and Synapse Development through Rho-Family GTPases and Cadherins

Cited by 192 publications

References 70 publications

p120catenin alteration in cancer and its role in tumour invasion

p120catenin alteration in cancer and its role in tumour invasion

p120-catenin is essential for maintenance of barrier function and intestinal homeostasis in mice

Essential cooperation of N-cadherin and neuroligin-1 in the transsynaptic control of vesicle accumulation

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