title: Rybp interacts with Hippi and enhances Hippi-mediated apoptosis.
abstract: Rybp (DEDAF) has been shown to interact with DED-containing proteins and to encode pro-apoptotic functions. Here we characterize a novel interaction between Rybp and Hippi, a protein implicated in neuronal apoptosis as well as in the pathogenesis of Huntington's disease. Rybp can synergize with Hippi to enhance Caspase 8-mediated apoptosis and also appears to be essential for Hippi-mediated apoptosis. Moreover, Rybp may mediate or regulate the interaction between Hippi and Caspase 8. Finally, Rybp and Hippi co-localize in a subset of neurons in the developing mouse brain. Together, these findings suggest that Rybp and Hippi may functionally interact in the apoptotic processes that accompany normal murine neural development.
authors.affiliation: Department of Molecular Genetics, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Ullmann 809, Bronx, NY 10461, USA. sstanton@aecom.yu.edu
authors.forename: Sasha E
authors.initials: SE
authors.lastname: Stanton
authors.forename: Jennifer K
authors.initials: JK
authors.lastname: Blanck
authors.forename: Joseph
authors.initials: J
authors.lastname: Locker
authors.forename: Nicole
authors.initials: N
authors.lastname: Schreiber-Agus
mesh_terms: D048868:Adaptor Proteins, Signal Transducing / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D000831:Animals, Newborn; D017209:Apoptosis; D001921:Brain / Q000166:cytology / Q000378:metabolism; D053181:Caspase 8 / Q000378:metabolism; D002460:Cell Line; D006801:Humans; D051379:Mice; D009474:Neurons / Q000166:cytology / Q000201:enzymology / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D012097:Repressor Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D048868:Adaptor Proteins, Signal Transducing; C449279:Esrrbl1 protein, mouse; D012097:Repressor Proteins; C120616:Rybp protein, mouse; D053181:Caspase 8