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Fostriecin, an antitumor antibiotic with inhibitory activity against serine/threonine protein phosphatases types 1 (PP1) and 2A (PP2A), is highly selective for PP2A
Author(s) -
Walsh Aimée H.,
Cheng Aiyang,
Honkanen Richard E.
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01210-6
Subject(s) - okadaic acid , protein phosphatase 2 , serine , threonine , phosphatase , chemistry , phosphorylation , biochemistry , pharmacology , biology
Fostriecin, an antitumor antibiotic produced by Streptomyces pulveraceus , is a strong inhibitor of type 2A (PP2A; IC 50 3.2 nM) and a weak inhibitor of type 1 (PP1; IC 50 131 μM) serine/threonine protein phosphatases. Fostriecin has no apparent effect on the activity of PP2B, and dose‐inhibition studies conducted with whole cell homogenates indicate that fostriecin also inhibits the native forms of PP1 and PP2A. Studies with recombinant PP1/PP2A chimeras indicate that okadaic acid and fostriecin have different binding sites.