response to "problems with lap nomenclature"
TRANSCRIPT
letters to the editor
NATURE CELL BIOLOGY VOL 3 APRIL 2001 http://cellbio.nature.comE90
Problems with LAP nomenclatureTo the editor —It was recently proposed1,2
that a group of cell-surface proteins withleucine-rich repeats (LRRs) and a PSD-95/Dlg/ZO-1 (PDZ) domain, which haveroles in epithelial cell shape and polarity, becollectively termed ‘LAP’ proteins (LRRand PDZ domain). This choice of name isinappropriate. 'LAP' is already used todesignate two leucine aminopeptidasegenes (LAP1 and LAP2), the herpesviruslatency-active promoter, and a liver acti-vating protein. Our direct concern is thatLAP also designates a family of lamin-associated polypeptides (LAPs) in thenuclear envelope, which were reported in1993. The term LAP has been used widelyin the nuclear envelope literature, appear-ing in over 36 papers since 1993. Thenuclear LAP1 and LAP2 genes encodealternatively spliced products (three andnine, respectively), many of which havedistinct nuclear localizations and func-tions. Further lamin-associated proteinsundoubtedly remain to be discovered, andinterest in this area is high because ofrecent discoveries linking a LAP2-relatedprotein, Emerin, to Emery–Dreifuss mus-cular dystrophy (EDMD), and linkinglamin mutations to at least three differentinherited diseases4,5. To avoid further confusion in the literature, we respectfullyurge you to discuss these problems withour PDZ domain colleagues, and encouragethem to choose a new, preferably four-let-ter name for LRR/PDZ domain proteinsthat does not duplicate a previously estab-lished name.Sincerely,
Katherine L. Wilson*, RicardoBenavente†, Brian Burke‡, Robert
Craigie§, Roland Foisner¶,Kazuhiro Furukawa#, Larry
Gerace**, Robert D. Goldman††,Yosef Gruenbaum‡‡, Crafford
Harris§§, Christopher J.Hutchison¶¶, Georg Krohne†,
Glenn E. Morris##, HenningOtto***, Amos J. Simon†††,
Howard J. Worman‡‡‡
*John Hopkins School of Medicine, Baltimore,USA; †University of Würzburg, Germany;
‡University of Calgary, Canada; §NationalInstitute of Health, Bethesda, Maryland, USA;
¶University of Vienna, Austria; #Niigata
University, Japan; **Scripps Research Institute,California, USA; ††Northwestern University
Medical School, Chicago, Illinois, USA; ‡‡HebrewUniversity of Jerusalem, Israel; §§R. W. Johnson
Pharmaceutical Research Institute, San Diego,California, USA;
¶¶University of Durham, UK; ***Freie UniversitatBerlin, Germany; ††† Chaim Sheba Medical
Center, Tel Hashomer Israel; ‡‡‡ColumbiaUniversity, New York, USA
1. Bilder et al. Nature Cell Biol. 2, E114 (2000).
2. Bryant, P.J. & Huwe, A. Nature Cell Biol. 2, E141–143 (2000).
3. Foisner, R. & Gerace, L. Cell 73, 1267–1279 (1993).
4. Wilson, K.L. Trends Cell Biol. 10, 125–129 (2000).
5. Bonne et al. Annals Neurol. 48, 170–180 (2000).
ResponseTo the editor — In calling attention to theseveral biomolecular entities whose nameshave been abbreviated ‘LAP’, Wilson et al.raise an important issue. Acronyms andsimilar abbreviations are beneficial for aterm that is used repeatedly in a publica-tion; however, the existence of multipleentities that use the same abbreviation cancause confusion. It is for this reason thatthe universal standard of journals calls forexplicit definition of an abbreviation at itsfirst usage in a paper. This technique servesto dispel ambiguity that might arise.In selecting an acronym for the leucine-rich repeat and PDZ-domain-containing(LAP) family of proteins, we searched the PubMed database, as well as the curat-ed LocusLink nomenclature database(www.ncbi.nlm.nih.gov/LocusLink/), forprevious uses of the abbreviation. As point-ed out by Wilson et al., LAP has been usedfor over 35 years to abbreviate the names ofindividual proteins (leucine aminopepti-dase, liver activating protein), a group ofunrelated proteins that share binding part-ners (lamin-associated polypeptides), andan inherited human disorder (laryngealadductor paralysis), as well as a gene-regu-latory element (latency-associated or activepromoter). We have used this acronym in adistinct, non-overlapping context: to
describe a structurally related protein fami-ly. Along with the initial explicit definition,the usage ‘LAP protein family’ serves to dis-tinguish the family of proteins that includesDensin-180, Scribble, Let-413 and ERBINfrom other biomolecules. Because this is adistinct usage we will continue to apply it.
David Bilder*, Daniel Birnbaum†,Jean-Paul Borg†, Jon Huibregtse‡,
Mary Kennedy§, MichelLabouesse¶, Bernard Mechler#,
Norbert Perrimon*
*Department of Genetics, Harvard MedicalSchool, Boston, Massachusetts, USA; †U119
INSERM, Molecular Oncology, Marseille, France;‡ICMB, University of Texas at Austin, Texas,
USA; §Division of Biology, California Institute ofTechnology, Pasedena, California, USA; ¶IGBMC,
CNRS/INSERM/ULP, Iukrich, France;#Developmental Genetics, Deutsches
Krebforshungs-Zentrum, Heidelberg, Germany
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Call for Letters to the Editor
LAP abbreviations
(LocusLink nomenclature database:www.ncbi.nlm.nih.gov/LocusLink/)
• Hyperlipidemia atherosclerosis prone
• Leucine aminopeptidase genes(LAP1 and LAP2)
• Herpesvirus latency active promoter
• Liver activating protien
• Lamin-associated polypeptides
• Leucine-rich repeat and a PDZdomain
• Laryngeal adductor paralysis
© 2001 Macmillan Magazines Ltd