This Correction updates and replaces the Expression of Concern (doi:10.1242/jcs.209973) relating to J. Cell Sci. (2002) 115, 3119-3130.

Journal of Cell Science was made aware of issues with this paper by a reader. Bands were duplicated in both the Myr and Palm blots in Fig. 1C. After discussion with the corresponding author, Ignacio Rodríguez-Crespo, the journal referred this matter to Universidad Complutense de Madrid (UCM). The UCM investigating committee reviewed replicate experiments to support the scientific results and conclusions, and found that Dr Rodríguez-Crespo did not include incorrect or fabricated data. They concluded: “…we believe that the scientific results and conclusions generated by the four papers overall are solid and do not become qualitatively invalidated by this manipulation of images…”.

The editorial policies of Journal of Cell Science state that: “Should an error appear in a published article that affects scientific meaning or author credibility but does not affect the overall results and conclusions of the paper, our policy is to publish a Correction…” and that a Retraction should be published when “…a published paper contain[s] one or more significant errors or inaccuracies that change the overall results and conclusions of the paper…”. We follow the guidelines of the Committee on Publication Ethics (COPE), which state: “Retraction should usually be reserved for publications that are so seriously flawed (for whatever reason) that their findings or conclusions should not be relied upon”. The standards of figure assembly and data presentation in this paper fall short of good scientific practice. However, given that the investigating committee at UCM decided that the conclusions of the paper were not affected by the errors, the appropriate course of action – according to COPE guidelines – is to publish a Correction.

The original data for the experiment shown in Fig. 1C were available and the correct figure panel is shown below. The new panel includes the entire gels as well as the running fronts with the radioactive labels.

Fig. 1.
Illustration of the linker-GFP construct with the location of the consensus myristoylation sequence and the positions where the mutations were introduced (A), expression of the recombinant proteins in COS-7 cells (B) and fatty acylation of the GFP chimeras (C). (C) Transfected COS-7 cells were starved for 1 hour in DMEM without serum and were then metabolically labeled for 4 hours with either [3H]-myristic acid (Myr) or [3H]-palmitic acid (Palm). Cell lysates were immunoprecipitated with an anti-GFP antibody, analyzed by SDS-PAGE and exposed to a film as described in the Materials and Methods. Identical results were obtained in two independent metabolic labeling experiments. 
View largeDownload slide

Illustration of the linker-GFP construct with the location of the consensus myristoylation sequence and the positions where the mutations were introduced (A), expression of the recombinant proteins in COS-7 cells (B) and fatty acylation of the GFP chimeras (C). (C) Transfected COS-7 cells were starved for 1 hour in DMEM without serum and were then metabolically labeled for 4 hours with either [3H]-myristic acid (Myr) or [3H]-palmitic acid (Palm). Cell lysates were immunoprecipitated with an anti-GFP antibody, analyzed by SDS-PAGE and exposed to a film as described in the Materials and Methods. Identical results were obtained in two independent metabolic labeling experiments. 

Fig. 1.
Illustration of the linker-GFP construct with the location of the consensus myristoylation sequence and the positions where the mutations were introduced (A), expression of the recombinant proteins in COS-7 cells (B) and fatty acylation of the GFP chimeras (C). (C) Transfected COS-7 cells were starved for 1 hour in DMEM without serum and were then metabolically labeled for 4 hours with either [3H]-myristic acid (Myr) or [3H]-palmitic acid (Palm). Cell lysates were immunoprecipitated with an anti-GFP antibody, analyzed by SDS-PAGE and exposed to a film as described in the Materials and Methods. Identical results were obtained in two independent metabolic labeling experiments. 
View largeDownload slide

Illustration of the linker-GFP construct with the location of the consensus myristoylation sequence and the positions where the mutations were introduced (A), expression of the recombinant proteins in COS-7 cells (B) and fatty acylation of the GFP chimeras (C). (C) Transfected COS-7 cells were starved for 1 hour in DMEM without serum and were then metabolically labeled for 4 hours with either [3H]-myristic acid (Myr) or [3H]-palmitic acid (Palm). Cell lysates were immunoprecipitated with an anti-GFP antibody, analyzed by SDS-PAGE and exposed to a film as described in the Materials and Methods. Identical results were obtained in two independent metabolic labeling experiments. 

The authors apologise to the journal and readers for these errors.

Journal of Cell Science refers readers to other Corrections related to the UCM investigation:

doi:10.1242/jcs.219667

doi:10.1242/jcs.219675

doi:10.1242/jcs.219683

View Original Article
© 2018. Published by The Company of Biologists Ltd
2018