Expression of p85α in bladder tumours and cell lines.

<p>A. Analysis of p85α mRNA expression levels in 105 bladder tumour samples and 52 normal bladder samples. Data from Sanchez-Carbayo et al [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0084411#B30" target="_blank">30</a>]. B. Quantitative analysis of p85α immunoblotted protein samples from bladder cancer cell lines normalized to tubulin and shown relative to pooled normal human urothelial cells (NHU-pool).</p

Distribution of <i>PIK3R1</i> mutations identified in UC.

<p>Distribution of <i>PIK3R1</i> mutations identified in UC.</p

Position of mutations in the p85α protein.

<p>A. Ribbon diagram of the structure of the complex of p110α with the niSH2 region of p85α (PDB code 2RD0) showing residues mutated in UC. B. Relationship of p85α nSH2 to p110α C2 domain showing proximity of N377 in nSH2 to C2 domain residue E365. C. Relationship of the iSH2 domain of p85α with the C2 domain of p110α showing proximity of R557 to N345 in C2. D. Space-filling model showing R481 and R557 residues in iSH2 of p85α in contact with C2 of p110α. E. Structure of p85 dimer (PDB code 1PBW) showing position of PIK3R1 point-mutated residues E137, R262 and K288 and the region deleted (W237-Y242) in UC in relation to residues involved in p85 dimerization (M176, dark green/light cyan; L161, I177 and V181, light green/cyan). The position of residue R274 (magenta), which is implicated in Rab-GAP activity is also shown. In addition, three glutamic acid residues (E266, E284 and E291) that interact with R262 are indicated, with E291 also interacting with K288. </p

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Figure S1. Protein expression analysis to aid in the molecular classification of breast cancer cell lines. Cell lysates containing equivalent amounts of total cell protein from the indicated non-tumorigenic breast (184B5, MCF10A, MCF10F, MCF12A) and breast cancer cell lines were probed with the indicated antibodies and GAPDH (loading control). The amount of total protein loaded per lane for each set of blots was as follows: ER (50 μg), PR (50 μg; PR-A is 81 kDa and PR-B is 116 kDa), HER2 (10 μg), EGFR (50 μg), p53 (50 μg), and GAPDH (50 μg). The molecular weight of each protein is indicated. (PDF 259 kb