Please wait a minute...

中国生物工程杂志

China Biotechnology
China Biotechnology  2012, Vol. 32 Issue (08): 1-8    DOI:
    
RIOK3 Promotes the Cleavage-activation of Caspase-10 on PAK2
LIN Ying, LI Pu, SHAN Jing-xuan, CHEN Xiao-jing, SHI Hui-li, HUO Ke-ke
State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University, Shanghai 200433, China
Download: HTML   PDF(1450KB) HTML
Export: BibTeX | EndNote (RIS)      

Abstract  RIO3, a member of atypical protein kinase, is only discovered in multicellular eukaryotes. The human liver cDNA library was screened with pDBLeu-RIOK3 as bait plasmid by yeast two-hybrid system and PAK2 was identified as a RIOK3 interactive protein. The interaction was confirmed by co-immunoprecipitation assays and immunofluorescent localization experiments. Results of real-time quantitative PCR and Western blot showed that RIOK3 can reduce the amount of PAK2 at protein expression level. CCK-8 and apoptosis detection experiment showed that co-expression of RIOK3 and PAK2 can inhibit cell proliferation and promote apoptosis,and the apoptotic effect can be inhibited by caspase-10G, which is the minimum isoform of caspase-10 and had no enzyme activity. The experimental results showed that RIOK3 may promote cleavage of caspase-10 on PAK2 and play an important role in the PAK2 cleavage-activation pathway.

Key wordsRIOK3      PAK2      Yeast two-hybrid system      Cell apoptotic      Cleavage-activation     
Received: 09 April 2012      Published: 25 August 2012
ZTFLH:  Q819  
Cite this article:

LIN Ying, LI Pu, SHAN Jing-xuan, CHEN Xiao-jing, SHI Hui-li, HUO Ke-ke. RIOK3 Promotes the Cleavage-activation of Caspase-10 on PAK2. China Biotechnology, 2012, 32(08): 1-8.

URL:

https://manu60.magtech.com.cn/biotech/     OR     https://manu60.magtech.com.cn/biotech/Y2012/V32/I08/1

[1] Angermayr M, Bandlow W. The type of basal promoter determines the regulated or constitutive mode of transcription in the common control region of the yeast gene pair GCY1/RIO1. J Biol Chem, 1997, 272(50): 31630-31635.
[2] Leonard C J, Aravind L, Koonin E V. Novel families of putative protein kinases in bacteria and archaea: evolution of the "eukaryotic" protein kinase superfamily. Genome Res, 1998, 8(10): 1038-1047.
[3] Angermayr M, Roidl A, Bandlow W. Yeast Rio1p is the founding member of a novel subfamily of protein serine kinases involved in the control of cell cycle progression. Mol Microbiol, 2002, 44(2): 309-324.
[4] Krupa A, Srinivasan N. Lipopolysaccharide phosphorylating enzymes encoded in the genomes of Gram-negative bacteria are related to the eukaryotic protein kinases. Protein Sci, 2002, 11(6): 1580-1584.
[5] Anaya P, Evans S C, Dai C, et al. Isolation of the Aspergillus nidulans sudD gene and its human homologue. Gene, 1998, 211(2): 323-329.
[6] LaRonde-LeBlanc N, Wlodawer A. A family portrait of the RIO kinases. J Biol Chem, 2005, 280(45): 37297-37300.
[7] LaRonde-LeBlanc N, Wlodawer A. The RIO kinases: an atypical protein kinase family required for ribosome biogenesis and cell cycle progression. Biochim Biophys Acta, 2005, 1754(1-2): 14-24.
[8] Geerlings T H, Faber A W, Bister M D, et al. Rio2p, an evolutionarily conserved, low abundant protein kinase essential for processing of 20 S Pre-rRNA in Saccharomyces cerevisiae. J Biol Chem, 2003, 278(25): 22537-22545.
[9] Scaffidi C, Krammer P H, Peter M E. Isolation and analysis of components of CD95 (APO-1/Fas) death-inducing signaling complex. Methods, 1999, 17(4): 287-291.
[10] Shan J, Wang P, Zhou J, et al. RIOK3 interacts with caspase-10 and negatively regulates the NF-kappaB signaling pathway. Mol Cell Biochem, 2009, 332(1-2): 113-120.
[11] Vanrobays E, Gelugne J P, Gleizes P E, et al. Late cytoplasmic maturation of the small ribosomal subunit requires RIO proteins in Saccharomyces cerevisiae. Mol Cell Biol, 2003, 23(6): 2083-2095.
[12] Luo S, Rubinsztein D C. Huntingtin promotes cell survival by preventing Pak2 cleavage. J Cell Sci, 2009, 122(Pt 6): 875-885.
[13] Kumar R, Gururaj A E, Barnes C J. p21-activated kinases in cancer. Nat Rev Cancer, 2006, 6(6): 459-471.
[14] Bokoch G M. Biology of the p21-activated kinases. Annu Rev Biochem, 2003, 72:743-781.
[15] Walter B N, Huang Z, Jakobi R, et al. Cleavage and activation of p21-activated protein kinase gamma-PAK by CPP32 (caspase 3). Effects of autophosphorylation on activity. J Biol Chem, 1998, 273(44): 28733-28739.
[16] Gatti A, Huang Z, Tuazon P T, et al. Multisite autophosphorylation of p21-activated protein kinase gamma-PAK as a function of activation. J Biol Chem, 1999, 274(12): 8022-8028.
[17] Jakobi R, McCarthy C C, Koeppel M A, et al. Caspase-activated PAK-2 is regulated by subcellular targeting and proteasomal degradation. J Biol Chem, 2003, 278(40): 38675-38685.
[18] Fischer U, Stroh C, Schulze-Osthoff K. Unique and overlapping substrate specificities of caspase-8 and caspase-10. Oncogene, 2006, 25(1): 152-159.
[19] Ng P W, Porter A G, Janicke R U. Molecular cloning and characterization of two novel pro-apoptotic isoforms of caspase-10. J Biol Chem, 1999, 274(15): 10301-10308.
[1] WANG Dan-dan, CHEN Tian, XU Liang-guo. Screening of VISA Interacting Proteins by Yeast Two-hybrid System[J]. China Biotechnology, 2017, 37(6): 63-69.
[2] LI Yao-feng, ZHANG Nan-yang, ZHAO Yong-ju. Methods of Construction and Identification of the Bait Vector in Yeast Two-Hybrid System[J]. China Biotechnology, 2012, 32(02): 123-127.
[3] . Preliminary Research on the Interaction between SSX2IP and 14-3-3η[J]. China Biotechnology, 2010, 30(07): 0-0.