J
Jörg Stappert
Researcher at Max Planck Society
Publications - 12
Citations - 4146
Jörg Stappert is an academic researcher from Max Planck Society. The author has contributed to research in topics: Catenin & Cadherin. The author has an hindex of 12, co-authored 12 publications receiving 4006 citations.
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Journal ArticleDOI
β‐catenin is a target for the ubiquitin–proteasome pathway
TL;DR: It is shown that ubiquitination of β‐catenin is greatly reduced in Wnt‐expressing cells, providing the first evidence that the ubiquitin–proteasome degradation pathway may act downstream of GSK3β in the regulation ofβ‐ catenin.
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Assembly of the cadherin-catenin complex in vitro with recombinant proteins
TL;DR: The reconstitution in vitro of the cadherin-catenin complex should allow the study of the interaction with signalling molecules and with the actin-based cytoskeleton.
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Brachyury is a target gene of the Wnt/β-catenin signaling pathway
Sebastian J. Arnold,Jörg Stappert,Andreas Bauer,Andreas Kispert,Bernhard G. Herrmann,Rolf Kemler +5 more
TL;DR: Results from a co-culture system consisting of NIH3T3 fibroblasts expressing different Wnts as feeder layer cells and embryonic stem cells expressing a green fluorescent protein (GFP) reporter gene transcriptionally regulated by the TCF/beta-catenin complex conclude that Brachyury is a target gene for Wnt/ beta-catin signaling.
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A short core region of E-cadherin is essential for catenin binding and is highly phosphorylated.
Jörg Stappert,Rolf Kemler +1 more
TL;DR: E-cadherin-catenin interaction may be regulated by phosphorylation of the catenin-binding domain, which might represent one molecular mechanism to regulate cadherin mediated cell adhesion.
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Casein Kinase II Phosphorylation of E-cadherin Increases E-cadherin/β-Catenin Interaction and Strengthens Cell-Cell Adhesion
TL;DR: Phosphorylation of the E-cadherin cytoplasmic domain by CKII and GSK-3β appears to modulate the affinity between β-catenin and E- cadhersin, ultimately modifying the strength of cell-cell adhesion.