Regulation of S33S37 phosphorylated βcatenin in normal and英文资料.pdfVIP

Research Article 2771 Regulation of S33/S37 phosphorylated β-catenin in normal and transformed cells 1, 1 1 2 2 2 Einat Sadot *, Maralice Conacci-Sorrell , Jacob Zhurinsky , Dalia Shnizer , Zeev Lando , Dorit Zharhary , 1 1 1,‡ Zvi Kam , Avri Ben-Ze’ev and Benjamin Geiger 1Department of Molecular Cell Biology, Weizmann Institute of Science Rehovot 76100 Israel 2Sigma Aldrich Israel, Park Rabin, Rehovot 76100, Israel *Present address: The Department of Ornamental Horticulture, The Volcani Center, Beit-Dagan, P.O.B. 6, 50250 Israel ‡Author for correspondence (e-mail: benny.geiger@weizmann.ac.il) Accepted 23 April 2002 Journal of Cell Science 115, 2771-2780 (2002) © The Company of Biologists Ltd Summary A novel phosphorylation-specific antibody (αpβ-catenin) form a ternary complex with DNA, suggesting that was generated against a peptide corresponding to amino it is transcriptionally inactive. Immunofluorescence acids 33-45 of human β-catenin, which contained microscopy indicated that pβ-catenin accumulates in the phosphorylated serines at positions 33 and 37. This nuclei of MDCK and BCAP cells when overexpressed and antibody is specific to phosphorylated β-catenin and reacts is transiently associated with adherens junctions shortly neither with the non-phosphorylated protein nor with after their formation. pβ-catenin only weakly interacts with phosphorylated or