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. 2010 Jul 6;123(15):2596–2604. doi: 10.1242/jcs.066514

Fig. 1.

Fig. 1.

Cell stress regulates association of hDlg with the splicing factors PSF and p54nrb. (A) Endogenous hDlg was immunoprecipitated, using 2 μg anti-hDlg antibody per sample, from 5 mg (lanes 1) or 10 mg (2) protein lysates from HEK293 cells, unstimulated or exposed to 0.5 M sorbitol (15 minutes). Protein bands a and b were excised from the gel, digested in-gel with trypsin, and their identity determined by mass fingerprinting. The number of peptides, percentage of sequence coverage and the accession number for each protein are given in the table. (B) Endogenous hDlg was immunoprecipitated, using 2 μg anti-hDlg antibody per sample, from 0.2 mg lysates from HEK293 or HeLa cells, unstimulated or stimulated as in A. Pellets were immunoblotted with anti-PSF or anti-p54nrb, with an antibody against hDlg phosphorylated at Ser158 (P-hDlgS158) and an antibody that recognises both unphosphorylated and phosphorylated hDlg.