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      A standardized kinesin nomenclature

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          Abstract

          In recent years the kinesin superfamily has become so large that several different naming schemes have emerged, leading to confusion and miscommunication. Here, we set forth a standardized kinesin nomenclature based on 14 family designations. The scheme unifies all previous phylogenies and nomenclature proposals, while allowing individual sequence names to remain the same, and for expansion to occur as new sequences are discovered.

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          Most cited references17

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          Basic local alignment search tool.

          A new approach to rapid sequence comparison, basic local alignment search tool (BLAST), directly approximates alignments that optimize a measure of local similarity, the maximal segment pair (MSP) score. Recent mathematical results on the stochastic properties of MSP scores allow an analysis of the performance of this method as well as the statistical significance of alignments it generates. The basic algorithm is simple and robust; it can be implemented in a number of ways and applied in a variety of contexts including straightforward DNA and protein sequence database searches, motif searches, gene identification searches, and in the analysis of multiple regions of similarity in long DNA sequences. In addition to its flexibility and tractability to mathematical analysis, BLAST is an order of magnitude faster than existing sequence comparison tools of comparable sensitivity.
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            The design plan of kinesin motors.

            The kinesin superfamily comprises a large and structurally diverse group of microtubule-based motor proteins that produce a variety of force-generating activities within cells. This review addresses how the structures of kinesin proteins provide clues as to their biological functions and motile properties. We discuss structural features common to all kinesin motors, as well as specialized features that enable subfamilies of related motors to carry out specialized activities. We also discuss how the kinesin motor domain uses chemical energy from ATP hydrolysis to move along microtubules.
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              Kinesin family in murine central nervous system

              In neuronal axons, various kinds of membranous components are transported along microtubules bidirectionally. However, only two kinds of mechanochemical motor proteins, kinesin and brain dynein, had been identified as transporters of membranous organelles in mammalian neurons. Recently, a series of genes that encode proteins closely related to kinesin heavy chain were identified in several organisms including Schizosaccharomyces pombe, Aspergillus niddulans, Saccharomyces cerevisiae, Caenorhabditus elegans, and Drosophila. Most of these members of the kinesin family are implicated in mechanisms of mitosis or meiosis. To address the mechanism of intracellular organelle transport at a molecular level, we have cloned and characterized five different members (KIF1-5), that encode the microtubule-associated motor domain homologous to kinesin heavy chain, in murine brain tissue. Homology analysis of amino acid sequence indicated that KIF1 and KIF5 are murine counterparts of unc104 and kinesin heavy chain, respectively, while KIF2, KIF3, and KIF4 are as yet unidentified new species. Complete amino acid sequence of KIF3 revealed that KIF3 consists of NH2-terminal motor domain, central alpha-helical rod domain, and COOH-terminal globular domain. Complete amino acid sequence of KIF2 revealed that KIF2 consists of NH2-terminal globular domain, central motor domain, and COOH-terminal alpha-helical rod domain. This is the first identification of the kinesin-related protein which has its motor domain at the central part in its primary structure. Northern blot analysis revealed that KIF1, KIF3, and KIF5 are expressed almost exclusively in murine brain, whereas KIF2 and KIF4 are expressed in brain as well as in other tissues. All these members of the kinesin family are expressed in the same type of neurons, and thus each one of them may transport its specific organelle in the murine central nervous system.
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                Author and article information

                Journal
                J Cell Biol
                The Journal of Cell Biology
                The Rockefeller University Press
                0021-9525
                1540-8140
                11 October 2004
                : 167
                : 1
                : 19-22
                Affiliations
                [1 ]Department of Plant Biology, The University of Georgia, Athens, GA 30602
                [2 ]Department of Genetics, The University of Georgia, Athens, GA 30602
                [3 ]These authors contributed equally to this work and are listed alphabetically
                [4 ]Department of Genetics, School of Medicine, Stanford University, Stanford, CA 94305
                [5 ]Ludwig Institute for Cancer Research, 3080 CMM-East, 9500 Gilman Drive, La Jolla, CA 92093
                [6 ]Department of Molecular and Cellular Biology, University of California, Berkeley, CA 94720
                [7 ]Department of Cell Biology, Duke University Medical Center, Durham, NC 27710
                [8 ]Department of Cellular and Molecular Medicine, Howard Hughes Medical Institute, School of Medicine, University of California, San Diego, La Jolla, CA 92093
                [9 ]Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46628
                [10 ]Department of Cell Biology and Anatomy, University of Tokyo, Graduate School of Medicine, Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan
                [11 ]Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany
                [12 ]Department of Molecular, Cellular and Developmental Biology, University of Colorado, Boulder, CO 80309
                [13 ]Institute for Chemistry and Cell Biology, Harvard Medical School, Boston, MA 02115
                [14 ]Department of Biology and Program in Cell and Molecular Biology, Colorado State University, Fort Collins, CO 80523
                [15 ]Department of Biology, Indiana University, Bloomington, IN 47405
                [16 ]Adolf-Butenandt-Institut, Zellbiologie, University of Munich, Schillerstr. 42, 80336 Munich, Germany
                [17 ]Center for Genetics and Development and Section of Molecular and Cellular Biology, University of California, Davis, CA 95616
                [18 ]Department of Cellular and Molecular Pharmacology, Howard Hughes Medical Institute, University of California, San Francisco, San Francisco, CA 94143
                [19 ]Department of Biochemistry and Molecular Biology, Indiana University Medical Sciences Program, Bloomington, IN 47405
                [20 ]Department of Physiology and Biophysics, University of Washington School of Medicine, Seattle, WA 98195
                Author notes

                Correspondence to Carolyn J. Lawrence: triffid@ 123456iastate.edu

                Article
                200408113
                10.1083/jcb.200408113
                2041940
                15479732
                e3bccd6e-129b-4be8-a24a-fcff879f3e10
                Copyright © 2004, The Rockefeller University Press
                History
                : 25 August 2004
                : 16 September 2004
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