This Correspondence is in response to a Commentary by Peter Lawrence in Nature on 20 March, 2003. Click here to read this article.
Sir – Congratulations to Peter A. Lawrence1 for his forceful denunciation in Commentary of the pernicious but pervasive view that publication in the 'right' journals is the same as publication of the best science. In particular, scientific editors who serve largely as postmen forwarding referees' comments to authors and expecting total compliance with referees' requests, however ill-judged, should respond to his plea that they revert to their proper function as judges both of the manuscript offered and of the referees' views. In my experience, there are still some proper editors, most often to be found on those learned-society-based journals that properly support their editors.
Lawrence elected “the original paper by Michael Berridge and Robin Irvine on phosphoinositol and cell signalling”, published in 1984, to show that the difficulties of publishing 'in the right place' are far from new. But in doing so he dived straight into the 'overcompression of information' trap that he rightly castigates. Rather than citing the first paper to establish the role of inositol 1,4,5-trisphosphate in Ca2+ signalling, he referred to a review that Berridge and Irvine wrote soon after. The original experimental paper2, also in Nature, had four authors, and was far from the 'original' paper on this topic. The entire field started in 1953 (ref. 3), and notions of the possible involvement of inositol lipids and phosphates in signalling reactions go back to the late 1960s (ref. 4).
My experiences in dealing with Nature during the decade leading up to ref. 2 were frustrating but sometimes, in the longer term, beneficial. Once the idea that phosphoinositide breakdown is implicated in cell signalling had grabbed us, we envisaged inositol 1:2-cyclic phosphate as a signal in stimulated cells in a paper in Nature New Biology5 — we were wrong. Two more steps were essential before Streb et al.2 could home in on the Ca2+-mobilizing action of inositol 1,4,5-trisphosphate. The first was to recognize a possibly causal relationship between receptor-driven phosphoinositide hydrolysis and Ca2+ mobilization6. Then we had to appreciate that receptor stimulation provokes PtdIns(4,5)P2 hydrolysis7,8 rather than the hydrolysis of PtdIns that we had previously postulated6. It was the latter discovery that identified Ins(1,4,5)P3 as the likely product of the receptor-regulated phospholipase.
Both of these advances were first submitted to Nature and were rejected without reaching referees. On each occasion I was in the fortunate position of having an immediate opportunity to expound the new idea in detail in an invited review or symposium paper. As a result, the first impact of each paper may have been slower, but availability of a more detailed initial exposition than could have appeared in a 'top' journal probably helped the ideas to be understood more readily.
References
Lawrence, P. A. Nature 422, 259–261 (2003).
Streb, H., Irvine, R. F., Berridge, M. J. & Schulz, I. Nature 306, 67–69 (1983).
Hokin, M. R. & Hokin, L. E. J. Biol. Chem. 203, 967–977 (1953).
Michell, R. H. in Phosphoinositides and Receptor Mechanisms (ed. Putney, J. W.) 1–24 (Alan R. Liss, New York, 1986).
Michell, R. H. & Lapetina, E. G. Nature New Biol. 240, 258–260 (1972).
Michell, R. H. Biochim. Biophys. Acta 415, 81–147 (1975).
Creba, J. A. et al. Biochem. J. 212, 733–747 (1983).
Michell, R. H. Phil. Trans. R. Soc. Lond. B 296, 123–138 (1981).
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Michell, B. Editors are meant to be judges, not postmen. Nature 423, 479–480 (2003). https://doi.org/10.1038/423479b
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DOI: https://doi.org/10.1038/423479b
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