Functional interaction between retinoblastoma protein and stress-activated protein kinase in multiple myeloma cells Journal Article


Authors: Chauhan, D.; Hideshima, T.; Treon, S.; Teoh, G.; Raje, N.; Yoshihimito, S.; Tai, Y. T.; Li, W.; Fan, J.; DeCaprio, J.; Anderson, K. C.
Article Title: Functional interaction between retinoblastoma protein and stress-activated protein kinase in multiple myeloma cells
Abstract: Previous studies have demonstrated that y-irradiation (IR)-induced apoptosis in multiple myeloma (MM) is associated with activation of stress- activated protein kinase (SAPK). In the present study, we examined the molecules downstream of SAPK/C-Jun N-terminal kinase (JNK), focusing on the role of retinoblastoma protein (Rb) during IR-induced MM cell apoptosis. The results demonstrate that IR activates SAPK/JNK, which associates with Rb both in vivo and in vitro. Far Western blot analysis confirms that SAPK/JNK binds directly to Rb. IR-activated SAPK/JNK phosphorylates Rb, and deletion of the phosphorylation site in the COOH terminus domain of Rb abrogates phosphorylation of Rb by SAPK/JNK. Taken together, our results suggest that Rb is a target protein of SAPK/JNK and that the association of SAPK/JNK and Rb mediates IR-induced apoptosis in MM cells.
Keywords: signal transduction; human cell; apoptosis; multiple myeloma; stress activated protein kinase; protein protein interaction; protein binding; enzyme activation; tumor cells, cultured; phosphorylation; gamma irradiation; mitogen-activated protein kinases; retinoblastoma protein; jnk mitogen-activated protein kinases; gamma rays; ca(2+)-calmodulin dependent protein kinase; humans; human; priority journal; article
Journal Title: Cancer Research
Volume: 59
Issue: 6
ISSN: 0008-5472
Publisher: American Association for Cancer Research  
Date Published: 1999-03-15
Start Page: 1192
End Page: 1195
Language: English
PUBMED: 10096546
PROVIDER: scopus
DOI/URL:
Notes: Article -- Export Date: 16 August 2016 -- Source: Scopus
Citation Impact
MSK Authors
  1. Weiwei Li
    63 Li
  2. Jianguo Fan
    30 Fan