Title : SHP-1 inhibits β-catenin function by inducing its degradation and interfering with its association with TATA-binding protein.

Pub. Date : 2011 Jan

PMID : 20840866






9 Functional Relationships(s)
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1 Tyrosine phosphorylation of beta-catenin is implicated as a means for its release from E-cadherin complexes and correlates with enhanced transcriptional activity. Tyrosine catenin beta 1 Homo sapiens
2 Herein, we demonstrate that inhibition of tyrosine phosphatases with pervanadate induced both c-src-dependent tyrosine phosphorylation and nuclear translocation of beta-catenin. Tyrosine catenin beta 1 Homo sapiens
3 Moreover, ectopic expression of SHP-1 but not the inactive form of SHP-1 (C453S) inhibited src-induced tyrosine phosphorylation of beta-catenin on tyrosines 86 and 654. Tyrosine catenin beta 1 Homo sapiens
4 Moreover, ectopic expression of SHP-1 but not the inactive form of SHP-1 (C453S) inhibited src-induced tyrosine phosphorylation of beta-catenin on tyrosines 86 and 654. Tyrosine catenin beta 1 Homo sapiens
5 SHP-1 expression and mutations of tyrosine-86 and tyrosine-654 to phenylalanine significantly and similarly decreased the transactivation potential of beta-catenin on the TOPFLASH reporter. Tyrosine catenin beta 1 Homo sapiens
6 SHP-1 expression as well as mutations of tyrosine-86 and tyrosine-654 to phenylalanine also significantly interfered with the association of beta-catenin with TBP. Tyrosine catenin beta 1 Homo sapiens
7 In conclusion, SHP-1 negatively regulates beta-catenin transcriptional activity i) by dephosphorylating beta-catenin on tyrosines 86 and 654, ii) by impairing its capacity to interact with the basal transcriptional factor TBP and iii) by promoting beta-catenin degradation in a GSK3beta-dependent manner. Tyrosine catenin beta 1 Homo sapiens
8 In conclusion, SHP-1 negatively regulates beta-catenin transcriptional activity i) by dephosphorylating beta-catenin on tyrosines 86 and 654, ii) by impairing its capacity to interact with the basal transcriptional factor TBP and iii) by promoting beta-catenin degradation in a GSK3beta-dependent manner. Tyrosine catenin beta 1 Homo sapiens
9 In conclusion, SHP-1 negatively regulates beta-catenin transcriptional activity i) by dephosphorylating beta-catenin on tyrosines 86 and 654, ii) by impairing its capacity to interact with the basal transcriptional factor TBP and iii) by promoting beta-catenin degradation in a GSK3beta-dependent manner. Tyrosine catenin beta 1 Homo sapiens