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. 2011 Mar 7;192(5):797–811. doi: 10.1083/jcb.201007014

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© 2011 Laursen et al.

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Figure 4. — hnRNP-K binds MBP mRNA. (A) Western blotting of lysates from oligodendrocytes generated by differentiation for 4 d on PDL or laminin after immunoprecipitation with hnRNP-K or control antibodies. The blot was developed with hnRNP-K antibody and confirms the specificity of the immunoprecipitation protocol. (B) Detection of MBP, PLP, myelin oligodendrocyte glycoprotein (MOG), or actin mRNA by RT-PCR after RNA immunoprecipitation as described in A. Note the high levels of MBP mRNA detected. (C) Quantification of mRNA levels for MBP, PLP, MOG, or actin after RNA immunoprecipitation of lysates from cells grown on laminin or PDL substrates with hnRNP-K or control antibodies, using input RNA isolated before immunoprecipitation as a reference. Values are means of three independent experiments ±SD. Statistical significance was tested by one-way ANOVA followed by a Tukey’s multiple comparison test. *, P < 0.05; **, P < 0.01; ***, P < 0.001. Note that only MBP mRNA levels are enhanced after hnRNP-K immunoprecipitation, and that these levels are reduced when the oligodendrocytes are cultured on laminin substrates. (D) Immunoprecipitation of hnRNP-K and tyrosine-phosphorylated proteins (shown in gel lanes labeled K and PY99, respectively, with the control input and IgG immunoprecipitation lanes also shown) from lysates of oligodendrocyte precursors (d 0, top blot) and mature oligodendrocytes (d 4, bottom blot) detected with antibodies against hnRNP-K. Note the increase in tyrosine phosphorylated hnRNP-K in mature cells cultured on laminin (Ln), as shown in the right-hand lane on the gel.

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