Rybp interacts with Hippi and enhances Hippi-mediated apoptosis.
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.
Stanton
Sasha E
SE
Department of Molecular Genetics, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Ullmann 809, Bronx, NY 10461, USA. sstanton@aecom.yu.edu
Blanck
Jennifer K
JK
Locker
Joseph
J
Schreiber-Agus
Nicole
N
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*
D048868:Adaptor Proteins, Signal Transducing; C449279:Esrrbl1 protein, mouse; D012097:Repressor Proteins; C120616:Rybp protein, mouse; D053181:Caspase 8