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      New consensus nomenclature for mammalian keratins

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          Abstract

          Keratins are intermediate filament–forming proteins that provide mechanical support and fulfill a variety of additional functions in epithelial cells. In 1982, a nomenclature was devised to name the keratin proteins that were known at that point. The systematic sequencing of the human genome in recent years uncovered the existence of several novel keratin genes and their encoded proteins. Their naming could not be adequately handled in the context of the original system. We propose a new consensus nomenclature for keratin genes and proteins that relies upon and extends the 1982 system and adheres to the guidelines issued by the Human and Mouse Genome Nomenclature Committees. This revised nomenclature accommodates functional genes and pseudogenes, and although designed specifically for the full complement of human keratins, it offers the flexibility needed to incorporate additional keratins from other mammalian species.

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          Most cited references 36

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          The catalog of human cytokeratins: patterns of expression in normal epithelia, tumors and cultured cells.

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            Comprehensive analysis of keratin gene clusters in humans and rodents.

            Here, we present the comparative analysis of the two keratin (K) gene clusters in the genomes of man, mouse and rat. Overall, there is a remarkable but not perfect synteny among the clusters of the three mammalian species. The human type I keratin gene cluster consists of 27 genes and 4 pseudogenes, all in the same orientation. It is interrupted by a domain of multiple genes encoding keratin-associated proteins (KAPs). Cytokeratin, hair and inner root sheath keratin genes are grouped together in small subclusters, indicating that evolution occurred by duplication events. At the end of the rodent type I gene cluster, a novel gene related to K14 and K17 was identified, which is converted to a pseudogene in humans. The human type II cluster consists of 27 genes and 5 pseudogenes, most of which are arranged in the same orientation. Of the 26 type II murine keratin genes now known, the expression of two new genes was identified by RT-PCR. Kb20, the first gene in the cluster, was detected in lung tissue. Kb39, a new ortholog of K1, is expressed in certain stratified epithelia. It represents a candidate gene for those hyperkeratotic skin syndromes in which no K1 mutations were identified so far. Most remarkably, the human K3 gene which causes Meesmann's corneal dystrophy when mutated, lacks a counterpart in the mouse genome. While the human genome has 138 pseudogenes related to K8 and K18, the mouse and rat genomes contain only 4 and 6 such pseudogenes. Our results also provide the basis for a unified keratin nomenclature and for future functional studies.
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              Inability of the acidic fibroblast growth factor mutant K132E to stimulate DNA synthesis after translocation into cells.

              Acidic fibroblast growth factor (aFGF) is a potent mitogen. It acts through activation of specific cell surface receptors leading to intracellular tyrosine phosphorylation cascades, but several reports also indicate that aFGF enters cells and that it has an intracellular function as well. The aFGF(K132E) mutant binds to and activates fibroblast growth factor receptors equally strongly as the wild-type, but it is a poor mitogen. We demonstrate that aFGF(K132E) enters NIH 3T3 cells and is transported to the nuclear fraction like wild-type aFGF. A fusion protein of aFGF(K132E) and diphtheria toxin A-fragment (aFGF(K132E)-DT-A) and a similar fusion protein containing wild-type aFGF (aFGF-DT-A) were reconstituted with diphtheria toxin B-fragment. Both fusion proteins were translocated to the cytosol by the diphtheria toxin pathway and subsequently recovered from the nuclear fraction. Whereas translocation of aFGF-DT-A stimulated DNA synthesis in U2OSDR1 cells lacking functional fibroblast growth factor receptors, aFGF(K132E)-DT-A did not. The mutation disrupts a protein kinase C phosphorylation site in the growth factor making it unable to be phosphorylated. The data indicate that a defect in the intracellular action of aFGF(K132E) is the reason for its strongly reduced mitogenicity, possibly due to inability to be phosphorylated.
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                Author and article information

                Affiliations
                [1 ]Section of Normal and Neoplastic Epidermal Differentiation, [2 ]Division of Cell Biology, German Cancer Research Center, 69120 Heidelberg, Germany
                [3 ]Department of Dermatology, School of Medicine, Cardiff University, Cardiff CF14 4XN, England, UK
                [4 ]Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205
                [5 ]Centre for Molecular Medicine, Singapore 13867
                [6 ]Division of Cell Biochemistry, Institute of Physiological Chemistry, University of Bonn, D-53115 Bonn, Germany
                [7 ]Mouse Genomic Nomenclature Committee, Mouse Genomic Informatics, The Jackson Laboratory, Bar Harbor, ME 04609
                [8 ]VA Palo Alto Health System and Stanford University School of Medicine, Department of Medicine, Palo Alto, CA 94304
                [9 ]Institute of Fundamental Sciences, Massey University, Palmerston North, New Zealand
                [10 ]Human Genome Organization Gene Nomenclature Committee, The Galton Laboratory, Department of Biology, University College London, London WC1E 6BT, England, UK
                Author notes

                Correspondence to Jürgen Schweizer: schweizer@ 123456dkfz.de

                Journal
                J Cell Biol
                JCB
                The Journal of Cell Biology
                The Rockefeller University Press
                0021-9525
                1540-8140
                17 July 2006
                : 174
                : 2
                : 169-174
                2064177
                200603161
                10.1083/jcb.200603161
                16831889
                Copyright © 2006, The Rockefeller University Press
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