Skip to main content
. 2021 Jun 7;12:3356. doi: 10.1038/s41467-021-23612-z

Fig. 2. Cyclin-CDKs form a stable dimeric complex that is further stabilized by p21/p27 binding.

Fig. 2

a Confocal fluorescence images of mVenus-cyclin D1 following photobleaching and dissociation from CDK4-mTurquoise-Δ50 lamin A complexes in cells depleted of p21 and p27 by siRNA-mediated co-knockdown. b Comparison of cyclin D1-CDK4 (n = 26 cells, 3 biological replicates), cyclin D1-CDK6 (n = 14 cells, 2 biological replicates) and cyclin E1-CDK2 (n = 18 cells, 3 biological replicates) mVenus-cyclin FRAP timecourses in cells depleted of p21 and p27. c mVenus-cyclin D1 FRAP timecourses in CDK4-mTurquoise-Δ50 lamin A complexes comparing cells depleted of p21 and p27 (n = 26, data from (b)) to cells co-transfected with mRuby3-p21 (n = 14 cells, 3 biological replicates) or mRuby3-p27 (n = 10 cells, 2 biological replicates). d mVenus-cyclin D1 FRAP timecourses in CDK6-mTurquoise-Δ50 lamin A complexes comparing cells depleted of p21 and p27 (n = 14; data (b)) to cells co-transfected with mRuby3-p21 (n = 15 cells, 3 biological replicates) or mRuby3-p27 (n = 13 cells, 2 biological replicates). e mRuby3-p21 (n = 14 cells, 3 biological replicates) or mRuby3-p27 (n = 14 cells, 3 biological replicates) FRAP timecourses in mVenus-cyclin D1 and CDK4-mTurquoise-Δ50 lamin A complexes. f mRuby3-p21 (n = 10 cells, 3 biological replicates) or mRuby3-p27 (n = 11 cells, 3 biological replicates) FRAP timecourses in mVenus-cyclin D1 and CDK6-mTurquoise-Δ50 lamin A complexes. FRAP timecourses show mean ± s.d. Source data are provided as a Source data file.