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

来源：

CHEMISTRY-AN ASIAN JOURNAL | 2008年 / 3卷 / 8-9期

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

页码：1607 / 1612

页数：6

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