Improvement of photoaffinity SPR Imaging platform and determination of the binding site of p62/SQSTM1 to p38 MAP kinase

被引:17
作者
Saito, Akiko [1 ]
Kawai, Kayoko [1 ,2 ]
Takayama, Hiroshi [1 ,2 ]
Sudo, Tatsuhiko [1 ]
Osada, Hiroyuki [1 ,2 ]
机构
[1] RIKEN, Adv Res Inst, Dept Biol Chem, Antibiot Lab, Wako, Saitama 3510198, Japan
[2] Saitama Univ, Grad Sch Sci & Engn, Saitama 3388570, Japan
关键词
biosensors; gold; peptides; photoaffinity labeling; surface plasmon resonance;
D O I
10.1002/asia.200800099
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
p38 mitogen-activated protein kinase (MAPK) is a member of the serine/threonine kinases and is activated in response to stress stimuli, such as cytokines, ultraviolet irradiation, heat shock, and osmotic shock. We revealed in a previous report that p62/SQSTM1, known to participate in proteasomal or autophagosomal protein degradation and cytokine receptor signal transduction pathways, binds to p38 to regulate specifically. Herein, we describe the improvement of the photoaffinity-thiol linker of our SPR imaging platform, which enabled us to determine the binding site of p62 to p38. SPR imaging experiments using a new photoaffinity linker 2 to immobilize the peptides derived from p62 on gold substrate indicate that the domain comprising amino acids 164-190 of p62 binds to p38 directly. These SPR analysis data and empirical biologic data reveal that the binding site of p62 to p38 is the domain corresponding to 173-182.
引用
收藏
页码:1607 / 1612
页数:6
相关论文
共 30 条
[11]  
KAWAI K, 2008, J BIOCH
[12]   Evaluation of MafG interaction with Maf recognition element arrays by surface plasmon resonance imaging technique [J].
Kyo, M ;
Yamamoto, T ;
Motohashi, H ;
Kamiya, T ;
Kuroita, T ;
Tanaka, T ;
Engel, JD ;
Kawakami, B ;
Yamamoto, M .
GENES TO CELLS, 2004, 9 (02) :153-164
[13]   Quantitative functional analysis of protein complexes on surfaces [J].
Lee, HJ ;
Yan, YL ;
Marriott, G ;
Corn, RM .
JOURNAL OF PHYSIOLOGY-LONDON, 2005, 563 (01) :61-71
[14]   Involvement of p38 mitogen-activated protein kinase signaling pathway in osteoclastogenesis mediated by receptor activator of NF-κB ligand (RANKL) [J].
Matsumoto, M ;
Sudo, T ;
Saito, T ;
Osada, A ;
Tsujimoto, M .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (40) :31155-31161
[15]   Surface plasmon resonance: towards an understanding of the mechanisms of biological molecular recognition [J].
McDonnell, JM .
CURRENT OPINION IN CHEMICAL BIOLOGY, 2001, 5 (05) :572-577
[16]   OXAZOLINES .11. SYNTHESIS OF FUNCTIONALIZED AROMATIC AND ALIPHATIC-ACIDS - USEFUL PROTECTING GROUP FOR CARBOXYLIC-ACIDS AGAINST GRIGNARD AND HYDRIDE REAGENTS [J].
MEYERS, AI ;
TEMPLE, DL ;
HAIDUKEW.D ;
MIHELICH, ED .
JOURNAL OF ORGANIC CHEMISTRY, 1974, 39 (18) :2787-2793
[17]   Antibody microarray profiling of human prostate cancer sera: Antibody screening and identification of potential biomarkers [J].
Miller, JC ;
Zhou, HP ;
Kwekel, J ;
Cavallo, R ;
Burke, J ;
Butler, EB ;
Teh, BS ;
Haab, BB .
PROTEOMICS, 2003, 3 (01) :56-63
[18]   Cell signaling and function organized by PB1 domain interactions [J].
Moscat, Jorge ;
Diaz-Meco, Maria T. ;
Albert, Armando ;
Campuzano, Sonsoles .
MOLECULAR CELL, 2006, 23 (05) :631-640
[19]   FORMATION OF SELF-ASSEMBLED MONOLAYERS BY CHEMISORPTION OF DERIVATIVES OF OLIGO(ETHYLENE GLYCOL) OF STRUCTURE HS(CH2)11(OCH2CH2)META-OH ON GOLD [J].
PALEGROSDEMANGE, C ;
SIMON, ES ;
PRIME, KL ;
WHITESIDES, GM .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1991, 113 (01) :12-20
[20]   Phosphotyrosine-independent binding of a 62-kDa protein to the src homology 2 (SH2) domain of p56(lck) and its regulation by phosphorylation of Ser-59 in the lck unique N-terminal region [J].
Park, I ;
Chung, J ;
Walsh, CT ;
Yun, YD ;
Strominger, JL ;
Shin, J .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (26) :12338-12342