Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the E-cadherin complex

By Yasuyuki Fujita, Gerd Krause, M. Scheffner, D. Zechner, H. M. Leddy, J. Behrens, T. Sommer, W. Birchmeier. Nature Cell Biology, 2002

891 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/72922cc730e19e9931199db9bcdd9f0a82a6a327

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

In Molecular Biology

Citations in the corpus

EMT, the cytoskeleton, and cancer cell invasion (2009, background): “Destabilization of the E-cadherin adhesion complex is also accomplished by receptor tyrosine kinase or Srcmediated phosphorylation of E-cadherin, followed by its ubiquitylation by the E3 ligase Hakai and subsequent degradation [57, 58] (Fig.”
A core function for p120-catenin in cadherin turnover (2003, background): “Candidates include presenilin-1 (Baki et al., 2001; Marambaud et al., 2002) and Hakai (Fujita et al., 2002), which are reported to compete with p120 for binding the cadherin juxtamembrane domain.”
Cadherins in development: cell adhesion, sorting, and tissue morphogenesis. (2006, positive): “It is targeted for internalization following ubiquitination by the E3 ubiquitin ligase Hakai (Figs. 2, 3; Fujita et al. 2002) and other pathways that involve disruption of the cadherin–catenin complex by tyrosine kinases (Kamei et al.”
The molecular mechanisms and therapeutic strategies of EMT in tumor progression and metastasis (2022, background): “Hakai, an E3 ubiquitin ligase, ubiquitinates E-cadherin, inducing its endocytosis and destruction [109].”
Cell adhesion and signalling by cadherins and Ig-CAMs in cancer (2004, background): “cgi?l=1000">(N)-cadherin , β-catenin, γ-catenin and p120-catenin, resulting in the disassembly of the CCC and, with it, the disruption of cadherin-mediated cell–cell adhesio”
Involvement of members of the cadherin superfamily in cancer. (2009, background): “Abnormal activation of proto-oncogenes, such as c-Met, Src, and EGFR, results in increased phosphorylation of tyrosine residues in the cytoplasmic domain of E-cadherin, which leads to recruitment of the E3-ubiquitin ligase Hakai and subsequently mediates internalization and ubiquitin-dependent degra”
Repression of E-cadherin by the polycomb group protein EZH2 in cancer (2008, background): “…repression by snail and slug, ubiquitination and degradation of the E-cadherin and lysosomal targeting of the E-cadherin for degradation (Batlle et al., 2000; Fujita et al., 2002; Hajra et al., 2002; Peinado et al., 2004; Saito et al., 2004; Takeno et al., 2004; Palacios et al., 2005).”
Invasive and Adherent Bacterial Pathogens Co-Opt Host Clathrin for Infection (2007, neutral): “However, no role for Cbl has been found in the internalization of E-cadherin ( Fujita et al., 2002 ).”
E-cadherin–integrin crosstalk in cancer invasion and metastasis (2013, background): “Early studies showed that oncogenic Src could control the endocytosis of E-cadherin (Fujita et al., 2002; Palacios et al., 2005).”
Epithelial-mesenchymal transition: at the crossroads of development and tumor metastasis. (2008, background): “Therefore, activation of tyrosine kinases in carcinoma cells could lead to rapid disruption of cell adhesion and a scattering phenotype (Fujita et al., 2002; Pece and Gutkind, 2002).”
New signals from the invasive front (2006, background): “RTKs, such as EGFR, c-Met, IGF-1R, FGF receptors (FGFRs) and the non-RTK c-Src can induce phosphorylation of E-cadherin and catenins, resulting in their ubiquitylation by the E3 ligase Hakai, and subsequent endocytosis and degradatio”