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. 1998 Feb 23;140(4):737–750. doi: 10.1083/jcb.140.4.737

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In vitro protein–protein interaction enhanced by SRPK-mediated phosphorylation. Bacterial GST-ASF/SF2 was phosphorylated by SRPK1 (lane 4) or SRPK2 (lane 6) or mock-phosphorylated (lanes 3 and 5). In vitro translated U1 70K (lane 1, total input in each binding assay) was incubated with beads coupled with GST or treated GST-ASF/SF2. Bound proteins were resolved in a 10% SDS-PAGE followed by autoradiography. (A) Coomassie blue staining of total (lane 1) and bound proteins (lanes 2–6). Note that phosphorylated GST-ASF/SF2 displayed a marked mobility shift. (B) An autoradiograph of the same protein gel. U1 70K was not retained by GST (lane 2), but bound to some extent to mock-phosphorylated GST-ASF/SF2 (lanes 3 and 5) and efficiently to phosphorylated GST-ASF/SF2 by SRPK1 (lane 4) and SRPK2 (lane 6).