Reference - Detail
| RRC ID | 28631 |
|---|---|
| Author | Saito A, Kawai K, Takayama H, Sudo T, Osada H. |
| Title | Improvement of photoaffinity SPR imaging platform and determination of the binding site of p62/SQSTM1 to p38 MAP kinase. |
| Journal | Chem Asian J |
| Abstract |
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. |
| Volume | 3(8-9) |
| Pages | 1607-12 |
| Published | 2008-9-1 |
| DOI | 10.1002/asia.200800099 |
| PMID | 18637653 |
| MeSH | Adaptor Proteins, Signal Transducing / analysis* Adaptor Proteins, Signal Transducing / chemistry Adaptor Proteins, Signal Transducing / metabolism* Binding Sites Cross-Linking Reagents / chemistry Molecular Structure Photoaffinity Labels / chemistry* Sulfhydryl Compounds / chemistry Surface Plasmon Resonance / methods* p38 Mitogen-Activated Protein Kinases / analysis* p38 Mitogen-Activated Protein Kinases / chemistry p38 Mitogen-Activated Protein Kinases / metabolism* |
| IF | 4.056 |
| Times Cited | 16 |
| WOS Category | CHEMISTRY, MULTIDISCIPLINARY |
| Resource | |
| DNA material | pGEX-hp38 (RDB08171) |