p120-catenin regulates VE-cadherin endocytosis and degradation induced by the Kaposi sarcoma–associated ubiquitin ligase K5

Nanes, Benjamin A.; Grimsley-Myers, Cynthia M.; Cadwell, Chantel M.; Robinson, Brian; Lowery, Anthony M.; Vincent, Peter; Mošunjac, Marina; Früh, Klaus; Kowalczyk, Andrew P.

doi:10.1091/mbc.e16-06-0459

Cited by 28 publications

(31 citation statements)

References 58 publications

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“…Endothelial HMEC-1 cells that express the K5 ligase by adenoviral transduction induce VE-cadherin ubiquitination and degradation, together with an increased internalization of VE-cadherin. Interestingly, K5-induced internalization of VE-cadherin does not depend on the same motif that drives the constitutive endocytosis of VE-cadherin, but p120 is still able to restrict the action of the K5 ligase, as the overexpression of p120 rescues K5-mediated down-regulation of VE-cadherin [62]. These data further corroborate the idea that the binding of p120 to the cadherin JMD acts as a master guardian of cadherins stability.…”

Section: Studies From Figueroa's Group Implicated Hakai In E-cadherinsupporting

confidence: 74%

“…One intriguing possibility is that a member of the membrane-associated really interesting new gene-CH family (MARCH) might serve such a function. Indeed, recent data demonstrated that VE-cadherin is a substrate of the human herpesvirus 8 ubiquitin ligase K5, a member of the MARCH family [62]. Endothelial HMEC-1 cells that express the K5 ligase by adenoviral transduction induce VE-cadherin ubiquitination and degradation, together with an increased internalization of VE-cadherin.…”

Section: Studies From Figueroa's Group Implicated Hakai In E-cadherinmentioning

confidence: 99%

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When ubiquitin meets E-cadherin: Plasticity of the epithelial cellular barrier

Niño

Sala

Polo

2019

Seminars in Cell & Developmental Biology

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A B S T R A C TCellular plasticity is, by definition, the ability of cells to adapt to a dynamic micro-environment by changing their phenotype. E-cadherin is the key organizer of the epithelial cell barrier, and it is required at the cell surface to preserve epithelial tissue integrity and homeostasis, since it not only organizes the adherens junctions, but also transfers intracellular signals that provide cues to regulate cell survival, morphology and polarity. As such, de-regulation of E-cadherin has deleterious effects on cells and whole tissues.The availability of cadherin at the cellular junctions is determined by the rates of new protein synthesis and degradation, as well as of internalization and recycling. Indeed, E-cadherin is subjected to a constant and a signal-mediated turnover due to trafficking and recycling between the cell surface and the cytoplasm. Importantly, the turnover of E-cadherin is required for both cell adhesion and cell plasticity within a tissue. Understanding the pathways and molecular mechanisms that E-cadherin undertakes to move in and out of adherens junctions, through which epithelial cells communicate with each other, has, thus, been a major research focus over the past decade, but several issues remain unresolved. Here, we review major advances and remaining open questions in the understanding of E-cadherin trafficking, with a particular focus on its ubiquitination. methionine residue on Ub allows the assembly of eight homotypic and

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Section: Studies From Figueroa's Group Implicated Hakai In E-cadherinsupporting

confidence: 74%

Section: Studies From Figueroa's Group Implicated Hakai In E-cadherinmentioning

confidence: 99%

When ubiquitin meets E-cadherin: Plasticity of the epithelial cellular barrier

Niño

Sala

Polo

2019

Seminars in Cell & Developmental Biology

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“…Second, it is important to distinguish between constitutive, vs regulated, cadherin endocytosis. For example, tyrosine phosphorylation of p120 ctn destabilizes its association with N‐cadherin to promote cadherin endocytosis in migrating astrocytes, while ubiquitination of VE‐cadherin promotes its endocytosis and downregulation in Kaposi sarcoma . Therefore, constitutive endocytosis may be tuned by both physiological and pathologic signals, and it will be essential to determine their functional contributions to tissue dynamics.…”

Section: Concluding Thoughts For the Futurementioning

confidence: 99%

Endocytosis, cadherins and tissue dynamics

Katsuno-Kambe

Yap

2020

Traffic

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By happy chance, the founding of Traffic in 1999 coincided with a clutch of reports that documented the endocytosis and recycling of classical cadherin adhesion receptors. This stimulated a concerted effort to elucidate the molecular regulation of cadherin endocytosis and to identify its functional implications. In particular, endocytosis provided new perspectives to understand how cadherins are modulated during tissue morphogenesis. In this short article, we consider some of what we have learnt about this problem and identify open questions for future research.

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“…In Madin‐Darby canine kidney (MDCK) II cells and human lung carcinomas, the E3 ligase Huwe1 facilitates poly‐Ub‐mediated degradation of the cadherin‐based adhesion mediator T‐cell lymphoma invasion and metastasis 1 (TIAM1), thereby promoting cell migration (Vaughan et al, ). The membrane‐associated really interesting new gene‐CH (MARCH) family E3 ligase, K5, could ubiquitinate vascular endothelial (VE)‐cadherin to promote its endocytosis and lysosomal degradation, thereby resulting in the disruption of endothelial AJs and remodelling of the actin cytoskeleton (Mansouri et al, ); however, p120 may prevent the vascular endothelial cadherin (VE‐cadherin) from taking part in K5 catalysis (Nanes et al, ). In herpes simplex virus 1 (HSV‐1)‐infected cells, the E3 ligase, Cbl, interacts with the cell adhesion molecule, Nectin‐1 to promote its removal from the membrane (Deschamps et al, ).…”

Section: Ubiquitination In Cellular Events Of Epithelial Morphogenesismentioning

confidence: 99%

Degradation for better survival? Role of ubiquitination in epithelial morphogenesis

Cheng

Zheng

et al. 2018

Biological Reviews

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As a prevalent post-translational modification, ubiquitination is essential for many developmental processes. Once covalently attached to the small and conserved polypeptide ubiquitin (Ub), a substrate protein can be directed to perform specific biological functions via its Ub-modified form. Three sequential catalytic reactions contribute to this process, among which E3 ligases serve to identify target substrates and promote the activated Ub to conjugate to substrate proteins. Ubiquitination has great plasticity, with diverse numbers, topologies and modifications of Ub chains conjugated at different substrate residues adding a layer of complexity that facilitates a huge range of cellular functions. Herein, we highlight key advances in the understanding of ubiquitination in epithelial morphogenesis, with an emphasis on the latest insights into its roles in cellular events involved in polarized epithelial tissue, including cell adhesion, asymmetric localization of polarity determinants and cytoskeletal organization. In addition, the physiological roles of ubiquitination are discussed for typical examples of epithelial morphogenesis, such as lung branching, vascular development and synaptic formation and plasticity. Our increased understanding of ubiquitination in epithelial morphogenesis may provide novel insights into the molecular mechanisms underlying epithelial regeneration and maintenance.

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p120-catenin regulates VE-cadherin endocytosis and degradation induced by the Kaposi sarcoma–associated ubiquitin ligase K5

Cited by 28 publications

References 58 publications

When ubiquitin meets E-cadherin: Plasticity of the epithelial cellular barrier

When ubiquitin meets E-cadherin: Plasticity of the epithelial cellular barrier

Endocytosis, cadherins and tissue dynamics

Degradation for better survival? Role of ubiquitination in epithelial morphogenesis

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