There was an error in J. Cell Sci. (2009) 122, 2034-2042 (doi:10.1242/jcs.038232).

A reader and the authors informed the journal that the left-hand western blots for pY397 and FAK were duplicated in Fig. 7A. The authors provided all the original data for Fig. 7 and explained that the wrong Y397 panel was used during preparation of the figure. The corrected figure is shown here.

Fig. 7 (corrected).

Integrin activation is necessary for the increase in FAK phosphorylation by Sema3A. (A) Hippocampal neurons from mouse embryos were cultured on PO and incubated at 3 d.i.v. with control medium or medium containing Sema3A for 20 minutes. MnCl2 (1 mM) was added together with the medium as indicated. Neurons were lysed and FAK phosphorylation was analysed by western blot (WB) using antibodies specific for FAK phosphorylated at Y397 or Y576/577. An anti-FAK antibody was used to confirm the loading of equivalent amounts of protein. (B) The quantification of FAK phosphorylation is shown as means±s.e.m.; *P<0.001 compared with control medium without MnCl2n=3.

Fig. 7 (corrected).

Integrin activation is necessary for the increase in FAK phosphorylation by Sema3A. (A) Hippocampal neurons from mouse embryos were cultured on PO and incubated at 3 d.i.v. with control medium or medium containing Sema3A for 20 minutes. MnCl2 (1 mM) was added together with the medium as indicated. Neurons were lysed and FAK phosphorylation was analysed by western blot (WB) using antibodies specific for FAK phosphorylated at Y397 or Y576/577. An anti-FAK antibody was used to confirm the loading of equivalent amounts of protein. (B) The quantification of FAK phosphorylation is shown as means±s.e.m.; *P<0.001 compared with control medium without MnCl2n=3.

The authors apologise to readers for this error, which does not impact the results or conclusions of the paper.