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. 2008 Sep 26;31(6):886–895. doi: 10.1016/j.molcel.2008.07.021

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© 2008 ELL & Excerpta Medica.

Open Access under CC BY 3.0 license

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Dephosphorylation of Cdc37p by Ppt1p in Yeast Extracts

(A) Cdc37p is phosphorylated on both S14 and S17 in yeast cell extracts. Immunoprecipitated (IP) Cdc37-HA and its S14A and S17A mutants were immunoblotted with anti-Phospho-Serine antibody.

(B) FLAG-tagged Ppt1p coimmunoprecipitates with the wild-type (WT), nonphosphorylatable (S14A/S17A), and phosphomimic (S14E/S17E) forms of HA-tagged Cdc37p.

(C) HA-tagged wild-type Cdc37p immunoprecipitated from cells overexpressing FLAG-tagged Ppt1p is substantially dephosphorylated, as are the single S14A and S17A phosphorylation-site mutants. Overexpression of Ppt1 has no effect on the phosphorylation of HA-tagged Cdc37p in cells expressing the nonphosphorylatable S14A/S17A mutant. A FLAG-tagged Ppt1p K81E/R85E mutant, which abrogates Ppt1 interaction with Hsp90, no longer dephosphorylates HA-tagged Cdc37p.