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Vol. 13, Issue 12, 4111-4113, December 2002




















*Center for Cell Signaling, University of Virginia School of
Medicine, Charlottesville, Virginia 22908;
Mouse Genome
Informatics, Jackson Laboratories, Bar Harbor, Maine 04609;
§Department of Cell Biology, Harvard Medical School,
Boston, Massachusetts 02115;
Research Institute of
Molecular Pathology, A-1030 Vienna, Austria; ¶Department
of Pediatrics, Graduate School of Medicine, University of Tokyo, Tokyo
113-8655, Japan; #Department of Cell Biology and
Neuroscience, Rutgers University, Piscataway, New Jersey 08854;
@Division of Biology, California Institute of Technology,
Pasadena, California 91125; **Department of Biochemistry and Molecular
Biology, Oklahoma State University, Stillwater, Oklahoma 74078;

Department of Biochemistry, University of Virginia
School of Medicine, Charlottesville, Virginia 22908;

Section of Psychiatry and Behavioral Sciences, Tokyo
Medical and Dental University Graduate School, 1-5-45, Yushima,
Bunkyo-ku, Tokyo 113-8519, Japan; §§Department of
Molecular Oncology, Kyoto University Graduate School of Medicine,
Yoshida Konoe-cho, Sakyo-ku, Kyoto 606-8501, Japan;

Department of Internal Medicine, University of
Michigan, Ann Arbor, Michigan 48109; ¶¶Department of
Biology, University of North Carolina, Chapel Hill, North Carolina
27599; ##Cell Signaling Unit, Children's Medical Research
Institute, Wentworthville 2145, New South Wales, Australia;
@@Max-Planck-Institute for Brain Research, Department of
Neurochemistry, Frankfurt, and Covidence GmbH, Philipp-Helfmann-Strasse
18, D-65760 Eschborn, Germany; ***Department of Oncology, Queen's
University of Belfast, Belfast BT9 7AB, United Kingdom;


Department of Biochemistry and Molecular Biology,
Mount Sinai School of Medicine, New York, New York 10029;


National Institute of Advanced Industrial Science
and Technology, Bldg. Tsukuba Central 6, Higashi, Tsukuba Science City,
Ibaraki 305-8566, Japan; §§§Tokai University
School of Medicine, Isehara, Kanagawa 259-1193, Japan;


Program in Cell Biology, Hospital for Sick
Children, University of Toronto, Toronto, Ontario M5G 1X8, Canada;
¶¶¶The Scripps Research Institute, La Jolla, California
92037; ###Cardinal Bernardin Cancer Center and Department
of Medicine, Loyola University Medical, Center, Maywood, Illinois
60153; and @@@Department of Pediatrics and
Adolescent Medicine, Children's Hospital, University of
Freiburg, D-79106 Freiburg, Germany
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ABSTRACT |
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There are 10 known mammalian septin genes, some of which produce multiple splice variants. The current nomenclature for the genes and gene products is very confusing, with several different names having been given to the same gene product and distinct names given to splice variants of the same gene. Moreover, some names are based on those of yeast or Drosophila septins that are not the closest homologues. Therefore, we suggest that the mammalian septin field adopt a common nomenclature system, based on that adopted by the Mouse Genomic Nomenclature Committee and accepted by the Human Genome Organization Gene Nomenclature Committee. The human and mouse septin genes will be named SEPT1-SEPT10 and Sept1-Sept10, respectively. Splice variants will be designated by an underscore followed by a lowercase "v" and a number, e.g., SEPT4_v1.
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ARTICLE |
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The septins are a family of proteins that were first discovered in the yeast Saccharomyces cerevisiae by analysis of mutants defective in cytokinesis and bud morphogenesis. It is now clear that they are widespread and probably ubiquitous in the fungi and animals, although apparently not in plants. Most if not all septins seem to bind and hydrolyze GTP and to participate in filament formation in vitro and probably in vivo. In addition to their widespread involvement in cytokinesis, the septins seem also to be involved in vesicle trafficking and other aspects of cell surface organization, and they may have other functions as well. For various trivial historical reasons, the current nomenclature for the mammalian septins is particularly chaotic and confusing. With the field still young but attracting increasing interest, there seems to be great value in rationalizing and simplifying the septin nomenclature at this time.
In accordance with the Mouse Genomic Nomenclature Committee
nomenclature, the mouse genes will be named Sept1-Sept10,
and the corresponding protein products will be SEPT1-SEPT10. Although these numbers do not correspond to the genetic distances between the
septins (Figure 1), they do provide an
unambiguous and consistent naming system. The Human Genome Organization
Gene Nomenclature Committee-approved symbols will be
SEPT1-SEPT10 for the genes, and the corresponding gene
products will be SEPT1-SEPT10. Although there are still too few
sequences available to be certain, it seems likely that most or all
septins of other vertebrates will prove to have unambiguous orthologues
among the mammalian septins, in which case it would be desirable to
name them by using the same system. For example, several fragments of
septin genes from frog and zebrafish are available in GenBank as
expressed sequence tags (ESTs), and these encode peptides that are
highly related to particular mammalian septins. Therefore, we suggest
that where possible other vertebrate septins be named using the same
system as used for the mammalian proteins. Usually, the species being described would be obvious from the context, but it could also be
indicated by adding, as a prefix, an abbreviation of the Latin binomial
for the species (e.g., Xl for Xenopus laevis).
For example, the frog septin A (GenBank no. AF212298), which is 89%
similar in sequence to human SEPT2 but only 61% similar to the next
most closely related human septin, would now be named Xl
SEPT2, or just SEPT2. (However, the prefix would not be a part of the
official gene symbol.) At the same time, comparison of the yeast,
Caenorhabditis elegans and Drosophila septins to
the mammalian septins (Adam, Peifer, and Pringle, unpublished data)
shows that the relationships are sufficiently complicated that the
mammalian nomenclature scheme could not reasonably be applied to
nonvertebrate septins.
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The proposed symbols are reconciled with the previously used aliases
for the mouse and human members of the septin family in Table
1. This table also provides selected
GenBank accession numbers for the mouse and human septins, the N- and
C-terminal sequences of the longest known variants (so as to provide an
unambiguous means of identification), and the human chromosome loci.
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Note that some septins currently have a multitude of distinct aliases
(e.g., SEPT9 names include Sint1, Sep9, E-septin, SLP-a, MSF, SepD1,
and Ov/Br septin), and SEPT6 has been named both Septin 6 and Sept2,
which engenders considerable confusion in the literature and in
database searches. Additionally, some vertebrate septins (e.g., Cdc10
or Pnutl) have been named after Saccharomyces cerevisiae or
Drosophila septins that are not true orthologues (or even
the closest homologues). Finally, at least four septin genes produce multiple splice variants, and these have also sometimes been given completely different names [e.g., SEPT4 splice variants include hCDCrel-2a, hCDCrel-2b, Bradeion-
and -B, ARTS, MART, and
Pnutl2(variants 1-4)]. To make the genetic origin of these variants
clear, we propose using the system adopted by the Mouse and Human
Genome Nomenclature Committees. In this system, splice variants are
distinguished by an underscore followed by a lowercase "v" and a
number, as listed in Table 1, e.g., the mouse G-septin
would
be named SEPT3_v1. Finally, we propose that if new, distinct septin
genes are discovered, they and their products be given a new number in
the sequence (e.g., SEPT11).
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FOOTNOTES |
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Corresponding author. E-mail address:
igm9c{at}virginia.edu.
Article published online ahead of print. Mol. Biol. Cell 10.1091/mbc.E02-07-0438. Article and publication date are at www.molbiolcell.org/cgi/doi/10.1091/mbc.E02-07-0438.
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