p120 Catenin-Associated Fer and Fyn Tyrosine Kinases Regulate β-Catenin Tyr-142 Phosphorylation and β-Catenin-α-Catenin Interaction

By J. Piedra, S. Miravet, J. Castaño, H. G. Pálmer, N. Heisterkamp, A. García de Herreros, M. Duñach. Molecular and Cellular Biology, 2003

319 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/46f8f2e1b0002c8f9db58435f2d6042c01bbcd6a

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In Cell Biology

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Citations in the corpus

• Balancing cell adhesion and Wnt signaling, the key role of β-catenin (2006, background): “It was shown that phosphorylation of these two key tyrosine residues leads to the disassembly of the E-cadherin–βcatenin–β-catenin complex at the plasma membrane and to increased β-catenin-dependent transcription (Fig.1) [43, 45 ,70,71,72].”
• Stability of dendritic spines and synaptic contacts is controlled by αN-catenin (2004, background): “The interactions between α-catenin and β-catenin can be altered by various factors, such as Fer and Fyn tyrosine kinases or protein kinase CKII, which affect their bindin”
• Cadherins and cancer: how does cadherin dysfunction promote tumor progression? (2008, background): “, 1999); and reduced binding of b-catenin to cadherin has been reported in growth factor- or oncogene-transformed cells (Piedra et al., 2003; Bamji et al., 2006).”
• Role of β-Catenin in Synaptic Vesicle Localization and Presynaptic Assembly (2003, unknown): “[PubMed: 11604139] Piedra J, Miravet S, Castano J, Palmer HG, Heisterkamp N, Garcia de Herreros A, Dunach M. p120 Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin Interaction.”
• The many faces and functions of β‐catenin (2012, unknown): “…Fyn, Fer, or the receptor tyrosine kinase c-Met 2720 The EMBO Journal VOL 31 | NO 12 | 2012 &2012 European Molecular Biology Organization significantly reduces a-catenin binding and thus impairs the adhesive function of b-catenin (Piedra et al, 2003; Brembeck et al, 2004; Bustos et al, 2006).”
• Tyrosine residues 654 and 670 in β-catenin are crucial in regulation of Met–β-catenin interactions (2006, background): “Conversely, inhibition of tyrosine phosphorylation can lead to reassociation of β-catenin to E-cadherin in rat-transformed cells [34,37].”