Phoslactomycin targets cysteine‐269 of the protein phosphatase 2A catalytic subunit in cells

• Takayuki Teruya

• Siro Simizu

• Naoki Kanoh

• Hiroyuki Osada

抄録

According to the chemical genetic approach, small molecules that bind directly to proteins are used to analyze protein function, thereby enabling the elucidation of complex mechanisms in mammal cells. Thus, it is very important to identify the molecular targets of compounds that induce a unique phenotype in a target cell. Phoslactomycin A (PLMA) is known to be a potent inhibitor of protein Ser/Thr phosphatase 2A (PP2A); however, the inhibitory mechanism of PP2A by PLMA has not yet been elucidated. Here, we demonstrated that PLMA directly binds to the PP2A catalytic subunit (PP2Ac) in cells by using biotinylated PLMA, and the PLMA‐binding site was identified as the Cys‐269 residue of PP2Ac. Moreover, we revealed that the Cys‐269 contributes to the potent inhibition of PP2Ac activity by PLMA. These results suggest that PLMA is a PP2A‐selective inhibitor and is therefore expected to be useful for future investigation of PP2A function in cells.

収録刊行物

• FEBS Letters

  FEBS Letters 579 (11), 2463-2468, 2005-03-31

  Wiley

キーワード

• Cell Biology
• Genetics
• Molecular Biology
• Biochemistry
• Structural Biology
• Biophysics

詳細情報

• CRID: 1360011142929968000
• NII論文ID: 80017279623
• DOI: 10.1016/j.febslet.2005.03.049
• ISSN: 18733468
• ISSN: 00145793
• Web Site: https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1016%2Fj.febslet.2005.03.049
• Web Site: https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/j.febslet.2005.03.049
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