Genomes and Genes
Affiliation: Serono Pharmaceutical Research Institute
- Yes-associated protein and p53-binding protein-2 interact through their WW and SH3 domainsX Espanel
Department of Biochemistry and Molecular Biology, Mount Sinai School of Medicine, New York, New York 10029 6574, USA
J Biol Chem 276:14514-23. 2001..Since overexpression of an activated form of c-Yes resulted in tyrosine phosphorylation of p53BP-2, we propose that the p53BP-2 phosphorylation, possibly in the WW1 domain-binding motif, might negatively regulate the YAP.p53BP-2 complex...
- Rsp5 WW domains interact directly with the carboxyl-terminal domain of RNA polymerase IIA Chang
Department of Biochemistry and Molecular Biology, New York University Mount Sinai School of Medicine, New York, New York 10029, USA
J Biol Chem 275:20562-71. 2000..In view of the recent data pertaining to phosphorylation-driven interactions between the RNA pol II CTD and the WW domain of Ess1/Pin1, we suggest that CTD dephosphorylation may be a prerequisite for targeted RNA pol II degradation...
- The WW domain of dystrophin requires EF-hands region to interact with beta-dystroglycanS Rentschler
Department of Biochemistry, Mount Sinai School of Medicine, New York, NY 10029, USA
Biol Chem 380:431-42. 1999..Targeted mutagenesis of conserved WW domain residues reveals that the dystrophin/beta-dystroglycan interaction occurs primarily through the WW domain of dystrophin. Precise mapping of this interaction could aid in therapeutic design...
- Pulling strings below the surface: hormone receptor signaling through inhibition of protein tyrosine phosphatasesX Espanel
Serono Pharmaceutical Research Institute, Geneva, Switzerland
Endocrine 15:19-28. 2001..In the present review, we outline this new paradigm for therapeutic regulation of the insulin receptor and discuss evidence that hints at other specific receptor-PTP pairs...