APH-1 is a Multipass Membrane Protein Essential for the Notch Signaling Pathway in Caenorhabditis elegans Embryos
Early embryonic cells in Caenorhabditis elegans embryos interact through a signaling pathway closely related to the Notch signaling pathway in Drosophila and vertebrates. Components of this pathway include a ligand, receptor, the presenilin proteins, and a novel protein, APH-2, that is related to th...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2002-01, Vol.99 (2), p.775-779 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Goutte, Caroline Tsunozaki, Makoto Hale, Valerie A. Priess, James R. |
| description | Early embryonic cells in Caenorhabditis elegans embryos interact through a signaling pathway closely related to the Notch signaling pathway in Drosophila and vertebrates. Components of this pathway include a ligand, receptor, the presenilin proteins, and a novel protein, APH-2, that is related to the Nicastrin protein in humans. Here we identify the aph-1 gene as a new component of the Notch pathway in Caenorhabditis elegans. aph-1 is predicted to encode a novel, highly conserved multipass membrane protein. We show that aph-1 and the presenilin genes share a similar function in that they are both required for proper cell-surface localization of APH-2/Nicastrin. |
| doi_str_mv | 10.1073/pnas.022523499 |
| format | Article |
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Components of this pathway include a ligand, receptor, the presenilin proteins, and a novel protein, APH-2, that is related to the Nicastrin protein in humans. Here we identify the aph-1 gene as a new component of the Notch pathway in Caenorhabditis elegans. aph-1 is predicted to encode a novel, highly conserved multipass membrane protein. 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Components of this pathway include a ligand, receptor, the presenilin proteins, and a novel protein, APH-2, that is related to the Nicastrin protein in humans. Here we identify the aph-1 gene as a new component of the Notch pathway in Caenorhabditis elegans. aph-1 is predicted to encode a novel, highly conserved multipass membrane protein. We show that aph-1 and the presenilin genes share a similar function in that they are both required for proper cell-surface localization of APH-2/Nicastrin.</description><subject>Alleles</subject><subject>Amino Acid Sequence</subject><subject>Amyloid Precursor Protein Secretases</subject><subject>Animals</subject><subject>aph-1 gene</subject><subject>APH-2 protein</subject><subject>Biological Sciences</subject><subject>Caenorhabditis elegans</subject><subject>Caenorhabditis elegans - embryology</subject><subject>Caenorhabditis elegans - genetics</subject><subject>Caenorhabditis elegans Proteins - genetics</subject><subject>Caenorhabditis elegans Proteins - physiology</subject><subject>Cell Membrane - physiology</subject><subject>Complementary DNA</subject><subject>Drosophila</subject><subject>Embryonic cells</subject><subject>Embryos</subject><subject>Genes</subject><subject>Genes, Helminth</subject><subject>Genetic mutation</subject><subject>Germ cells</subject><subject>Helminth Proteins - genetics</subject><subject>Helminth Proteins - physiology</subject><subject>Homeodomain Proteins - genetics</subject><subject>Homeodomain Proteins - physiology</subject><subject>Membrane Glycoproteins - genetics</subject><subject>Membrane Glycoproteins - physiology</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - physiology</subject><subject>Membranes</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Nicastrin</subject><subject>Pharynx</subject><subject>Phenotype</subject><subject>presenilin gene</subject><subject>Presenilins</subject><subject>Proteins</subject><subject>Receptors, Notch</subject><subject>Sequence Homology, Amino Acid</subject><subject>Signal Transduction</subject><subject>Somatic cells</subject><subject>Worms</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1vEzEQxVcIRNPClRNCFlK5bfDnen3ooYoCRWohEnC2ZjferCNnndpeIP89jhJS4ACnObzfe5qZVxQvCJ4SLNnb7QBxiikVlHGlHhUTghUpK67w42KCMZVlzSk_K85jXGOMlajx0-KMEKlozatJcX-9uCkJshEBuhtdsluIEd2ZTRNgMGgRfDJ2QPMYzZAsONT5gFJv0Eef2h59tqsBnB1WaAGp_w47lOEZmMGHHpqlTTnYOLOCIaJ5ztz5-Kx40oGL5vlxXhRf382_zG7K20_vP8yub8tWEJHKrsIgDWG4a1RnWF1BLWSzVFRhwkTFOwLAO2hpJ1XNoRLZ0DSkFjTDS8zYRXF1yN2OzcYs27x_AKe3wW4g7LQHq_9UBtvrlf-m83NYTbL_zdEf_P1oYtIbG1vjXP6LH6OWhBOMhfwvSGrK5AF8_Re49mPI_4ua5qNUXan92tMD1AYfYzDdaWOC9b5yva9cnyrPhle_3_mAHzvOwMsjsDf-kpXSVEspsnz5D1l3o3PJ_EgPMeuYfDiBLF9WccJ-AjTTyHk</recordid><startdate>20020122</startdate><enddate>20020122</enddate><creator>Goutte, Caroline</creator><creator>Tsunozaki, Makoto</creator><creator>Hale, Valerie A.</creator><creator>Priess, James R.</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><general>The National Academy of Sciences</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20020122</creationdate><title>APH-1 is a Multipass Membrane Protein Essential for the Notch Signaling Pathway in Caenorhabditis elegans Embryos</title><author>Goutte, Caroline ; Tsunozaki, Makoto ; Hale, Valerie A. ; Priess, James R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c515t-f60a7e130fb9fe386a857bd929013564f1aa4fac2f7984a65f60bb1852e38d033</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Alleles</topic><topic>Amino Acid Sequence</topic><topic>Amyloid Precursor Protein Secretases</topic><topic>Animals</topic><topic>aph-1 gene</topic><topic>APH-2 protein</topic><topic>Biological Sciences</topic><topic>Caenorhabditis elegans</topic><topic>Caenorhabditis elegans - embryology</topic><topic>Caenorhabditis elegans - genetics</topic><topic>Caenorhabditis elegans Proteins - genetics</topic><topic>Caenorhabditis elegans Proteins - physiology</topic><topic>Cell Membrane - physiology</topic><topic>Complementary DNA</topic><topic>Drosophila</topic><topic>Embryonic cells</topic><topic>Embryos</topic><topic>Genes</topic><topic>Genes, Helminth</topic><topic>Genetic mutation</topic><topic>Germ cells</topic><topic>Helminth Proteins - genetics</topic><topic>Helminth Proteins - physiology</topic><topic>Homeodomain Proteins - genetics</topic><topic>Homeodomain Proteins - physiology</topic><topic>Membrane Glycoproteins - genetics</topic><topic>Membrane Glycoproteins - physiology</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - physiology</topic><topic>Membranes</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Nicastrin</topic><topic>Pharynx</topic><topic>Phenotype</topic><topic>presenilin gene</topic><topic>Presenilins</topic><topic>Proteins</topic><topic>Receptors, Notch</topic><topic>Sequence Homology, Amino Acid</topic><topic>Signal Transduction</topic><topic>Somatic cells</topic><topic>Worms</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Goutte, Caroline</creatorcontrib><creatorcontrib>Tsunozaki, Makoto</creatorcontrib><creatorcontrib>Hale, Valerie A.</creatorcontrib><creatorcontrib>Priess, James R.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Goutte, Caroline</au><au>Tsunozaki, Makoto</au><au>Hale, Valerie A.</au><au>Priess, James R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>APH-1 is a Multipass Membrane Protein Essential for the Notch Signaling Pathway in Caenorhabditis elegans Embryos</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2002-01-22</date><risdate>2002</risdate><volume>99</volume><issue>2</issue><spage>775</spage><epage>779</epage><pages>775-779</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Early embryonic cells in Caenorhabditis elegans embryos interact through a signaling pathway closely related to the Notch signaling pathway in Drosophila and vertebrates. Components of this pathway include a ligand, receptor, the presenilin proteins, and a novel protein, APH-2, that is related to the Nicastrin protein in humans. Here we identify the aph-1 gene as a new component of the Notch pathway in Caenorhabditis elegans. aph-1 is predicted to encode a novel, highly conserved multipass membrane protein. We show that aph-1 and the presenilin genes share a similar function in that they are both required for proper cell-surface localization of APH-2/Nicastrin.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>11792846</pmid><doi>10.1073/pnas.022523499</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 2002-01, Vol.99 (2), p.775-779 |
| issn | 0027-8424 1091-6490 |
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| subjects | Alleles Amino Acid Sequence Amyloid Precursor Protein Secretases Animals aph-1 gene APH-2 protein Biological Sciences Caenorhabditis elegans Caenorhabditis elegans - embryology Caenorhabditis elegans - genetics Caenorhabditis elegans Proteins - genetics Caenorhabditis elegans Proteins - physiology Cell Membrane - physiology Complementary DNA Drosophila Embryonic cells Embryos Genes Genes, Helminth Genetic mutation Germ cells Helminth Proteins - genetics Helminth Proteins - physiology Homeodomain Proteins - genetics Homeodomain Proteins - physiology Membrane Glycoproteins - genetics Membrane Glycoproteins - physiology Membrane Proteins - genetics Membrane Proteins - physiology Membranes Molecular Sequence Data Mutation Nicastrin Pharynx Phenotype presenilin gene Presenilins Proteins Receptors, Notch Sequence Homology, Amino Acid Signal Transduction Somatic cells Worms |
| title | APH-1 is a Multipass Membrane Protein Essential for the Notch Signaling Pathway in Caenorhabditis elegans Embryos |
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