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. 1999 Sep;10(9):2971–2986. doi: 10.1091/mbc.10.9.2971

Figure 1.

Figure 1

Mutation to alanine of six phosphorylatable residues in p90rsk impairs its activation by progesterone and its ability to dissociate from p42mpk1. (A) Lysates were prepared from untreated or progesterone-treated oocytes expressing either myc-tagged p90rsk or p90rsk (6xA) and were analyzed by immunoblotting using anti-myc and anti-p42mpk1, as indicated. Anti-myc immunoprecipitates were prepared from the same oocyte lysates, and their associated kinase activity was assayed using GST-Myt1 as an in vitro substrate. (B) Lysates were prepared from either untreated or progesterone-treated oocytes expressing the indicated p90rsk and p42mpk1 proteins and were immunoprecipitated with anti-p42mpk1 antibodies. The total lysates (lanes 1–8) and the anti-p42mpk1 immunoprecipitates (lanes 9–16) were analyzed by immunoblotting with anti-p90rsk and anti-myc antibodies.