Supplemental Figure 1
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1 Supplemental Figure 1 A C19 B Mα p27 TL p27-/- p27-/- Supplemental Figure 1: Altered expression of p27 and p27 in the brain. Immunostaining for p27 was performed on brain frozen sections. Brain sections were stained with a polyclonal anti-p27 (C19) antibody (A) or with a monoclonal anti-p27 (clone 57, BD-Transduction Laboratories (TL)) antibody (B). Note that the latter antibody does not recognize p27.
2 Supplemental Figure 2 CHX + Olo + Rosco CHX + Olo + Rosco CHX + Olo + Rosco Supplemental Figure 3: CDK inhibition does not prevent p27 degradation in G0. Wild type or p27 were serum starved for 72 h, cells were treated with 25 µg/ml cycloheximide (CHX) and, where indicated, with 50 µm Olomoucine or Roscovitine. Lysates were collected in sample buffer at the indicated time. Samples were resolved on SDS-PAGE, transferred and membranes were probed with a polyclonal p27 antibody (C19), stripped and reprobed with a monoclonal Grb2 antibody to evaluate protein loading.
3 Supplemental Figure 3 Cyclin D1-/- Cyclin E1/E2-/- Cyclin D1/D2-/- CDK2-/- CDK4-/- Supplemental Figure 4: p27 half-life in G0 is not affected by the absence of specific cyclins or CDKs. Cyclin D1 -/-, cyclin D1/D2 -/-, cyclin E1/E2 -/-, CDK2 -/-, CDK4 -/- and their corresponding wild type MEFs were serum starved for 72 h, cells were treated with 25 µg/ml cycloheximide (CHX) and collected in sample buffer at the indicated time. Samples were resolved on SDS-PAGE, transferred and membranes were probed with a polyclonal p27 antibody (C19), stripped and reprobed with a monoclonal Grb2 antibody to evaluate protein loading. Cyclin D1 -/-, cyclin D1/D2 -/-, cyclin E1/E2 -/- MEFs were kindly provided by Piotr Sicinsky, Dana Farber Cancer Institute, Boston. CDK2 -/- MEFs were kindly provided by Philipp Kaldis, National Cancer Institute, Frederick. CDK4 -/- MEFs were a gift from Hiroaki Kiyokawa, University of Illinois College of Medicine, Chicago.
4 Supplemental Figure 4 Exponentially growing cells p27-/- pqh-p27 p27-/- pqh- p27-/- pqh-/ CHX in h Supplemental Figure 2: Stabilization of a p27 mutant that cannot bind cyclins and CDKs (p27 /) in exponentially growing cells. p27-null MEFs were retrovirally infected with either wild type p27 (p27-/-lnsx-p27), p27 (p27-/-pqh-), or p27 / (p27-/-lnsx-/). After selection of infected MEFs, cells were treated with 25 µg/ml cycloheximide (CHX) and collected in sample buffer at the indicated time. Samples were resolved on SDS-PAGE, transferred and membranes were probed with a polyclonal p27 antibody (C19), stripped and reprobed with a monoclonal Grb2 antibody to evaluate protein loading.
5 Supplemental Figure 5 A Serum starved IP Rα Cyclin A (H432) Exponentially growing Mα p27f8 B Serum starved IP Rα Cyclin E Exponentially growing Mα p27f8 Mα CDK2 Supplemental Figure 5: Increased association of p27 with cyclin-cdk complexes. IPs with a polyclonal cyclin A antibody (A) or with a polyclonal cyclin E antibody (B) in serum starved and exponentially growing primary MEFs. Membranes were probed with a monoclonal antibody to p27. In B, the membrane was reprobed with a monoclonal CDK2 anitbody.
6 Supplemental Figure 6 A Mα p27 Hoescht 0.1% FCS B 0.1% FCS 10% FCS 4 h 10% FCS 8 h +MG132 +MG132 Supplemental Figure 6: p27 is sequestered in the nucleus. In this experiment, wild type and p27 -/- cells were co-cultured, thus providing an internal control for non-specific staining by the p27 antibody. Exposure time was set so that the p27 -/- barely appear on the images, and the same setting was used to acquire all the images. A. monoclonal p27 antibody stain of wild type and p27 -/- MEFs (left) and Hoescht stain to visualize the nuclei of both cell types (right); wild type cells are indicated by arrowheads (right). B. Staining with the monoclonal p27 antibody as in (A) of wild type, p27 -/-, and p27 MEFs either serum starved for 48 h, or starved and stimulated with 10% FCS for 4 h or 8 h, in the presence or absence of the proteasome inhibitor MG132.
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