Fudan University Journal of Medical Sciences

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Research progress on p120-catenin in vascular development and endothelial barrier function

Xi XUE, Yi-wen MAO, Ming-jie WANG

Fudan University Journal of Medical Sciences, 2025, 52(04): 572-580. DOI: 10.3969/j.issn.1672-8467.2025.04.015

Fig 4 Kaiso transcription factor and its binding partner p120ctn Kaiso nuclear export mediates by phosphorylated p120ctn is currently only reported in p120ctn subtype 3. However, phosphorylation of both p120ctn subtypes 1 and 3 by CK1 have been observed to upregulate the binding of p120ctn with Kaiso. This figure is created with BioGDP.com^[5].

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Fig 1 The structure of p120-catenin The p120ctn consists of four structural domains from the N-terminus to the C-terminus. It includes coiled-coil domain, regulatory domain, 10 Armadillo protein repeats and C-terminal domain^[1].This figure is created with BioGDP.com^[5].
Fig 2 p120ctn and its interacting proteins Adherens junctions are mainly composed of two parts: VE-cadherin and catenins. P120ctn is the primary factor that promotes the stability of VE-cadherin. This figure is created with BioGDP.com^[5].
Fig 3 The core p120ctn-binding region of VE-cadherin GGG is the core binding site of p120ctn in VE-cadherin. DEE is the core site of VE-cadherin endocytosis. Widely used experimental mutants of either binding site are also shown. This figure is created with BioGDP.com^[5].

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