Membrane guanylate cyclase is a cell-surface receptor with homology to protein kinases
Guanylate cyclase has been strongly implicated as a cell-surface receptor on spermatozoa for a chemotactic peptide, and on various other cells as a receptor for atrial natriuretic peptides. Resact (Cys-Val-Thr-Gly-Ala-Pro-Gly-Cys-Val-Gly-Gly-Gly-Arg-Leu-NH2), the chemotactic peptide released by sea...
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| Veröffentlicht in: | Nature (London) 1988-08, Vol.334 (6184), p.708-712 |
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| container_title | Nature (London) |
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| creator | SUJAY SINGH LOWE, D. G THORPE, D. S RODRIGUEZ, H WUN-JING KUANG DANGOTT, L. J CHINKERS, M GOEDDEL, D. V GARBERS, D. L |
| description | Guanylate cyclase has been strongly implicated as a cell-surface receptor on spermatozoa for a chemotactic peptide, and on various other cells as a receptor for atrial natriuretic peptides. Resact (Cys-Val-Thr-Gly-Ala-Pro-Gly-Cys-Val-Gly-Gly-Gly-Arg-Leu-NH2), the chemotactic peptide released by sea urchin Arbacia punctulata eggs, is specifically crosslinked to A. punctulata spermatozoan guanylate cyclase. After the binding of the peptide the state of guanylate cyclase phosphorylation modulates enzyme activity. We report here that the deduced amino-acid sequence of the spermatozoan membrane form of guanylate cyclase predicts an intrinsic membrane protein of 986 amino acids with an amino-terminal signal sequence. A single transmembrane domain separates the protein into putative extracellular and cytoplasmic-catalytic domains. The cytoplasmic carboxyl-terminal 95 amino acids contain 20% serine, the likely regulatory sites for phosphorylation. Unexpectedly, the enzyme is homologous to the protein kinase family. |
| doi_str_mv | 10.1038/334708a0 |
| format | Article |
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G ; THORPE, D. S ; RODRIGUEZ, H ; WUN-JING KUANG ; DANGOTT, L. J ; CHINKERS, M ; GOEDDEL, D. V ; GARBERS, D. L</creator><creatorcontrib>SUJAY SINGH ; LOWE, D. G ; THORPE, D. S ; RODRIGUEZ, H ; WUN-JING KUANG ; DANGOTT, L. J ; CHINKERS, M ; GOEDDEL, D. V ; GARBERS, D. L</creatorcontrib><description>Guanylate cyclase has been strongly implicated as a cell-surface receptor on spermatozoa for a chemotactic peptide, and on various other cells as a receptor for atrial natriuretic peptides. Resact (Cys-Val-Thr-Gly-Ala-Pro-Gly-Cys-Val-Gly-Gly-Gly-Arg-Leu-NH2), the chemotactic peptide released by sea urchin Arbacia punctulata eggs, is specifically crosslinked to A. punctulata spermatozoan guanylate cyclase. After the binding of the peptide the state of guanylate cyclase phosphorylation modulates enzyme activity. We report here that the deduced amino-acid sequence of the spermatozoan membrane form of guanylate cyclase predicts an intrinsic membrane protein of 986 amino acids with an amino-terminal signal sequence. A single transmembrane domain separates the protein into putative extracellular and cytoplasmic-catalytic domains. The cytoplasmic carboxyl-terminal 95 amino acids contain 20% serine, the likely regulatory sites for phosphorylation. Unexpectedly, the enzyme is homologous to the protein kinase family.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/334708a0</identifier><identifier>PMID: 2901039</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing</publisher><subject>Amino Acid Sequence ; Amino acids ; Animals ; Base Sequence ; Biological and medical sciences ; Cell Membrane - enzymology ; Cell receptors ; Cell structures and functions ; Cellular biology ; DNA - genetics ; DNA, Recombinant ; Enzymatic activity ; Fundamental and applied biological sciences. Psychology ; Genetics ; Glycosylation ; Guanylate Cyclase - genetics ; Guanylate Cyclase - isolation & purification ; Humans ; Male ; Medical research ; Membranes ; Mice ; Molecular and cellular biology ; Molecular Sequence Data ; Peptides ; Protein Kinases ; Proteins ; Receptors, Cell Surface ; Sea Urchins ; Sequence Homology, Nucleic Acid ; Spermatozoa - enzymology</subject><ispartof>Nature (London), 1988-08, Vol.334 (6184), p.708-712</ispartof><rights>1989 INIST-CNRS</rights><rights>Copyright Macmillan Journals Ltd. Aug 25, 1988</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c365t-dfddff29aaedf4f5383cc0970e9ba9d51e99e6e9027d18bd3c2f75d36857f37f3</citedby><cites>FETCH-LOGICAL-c365t-dfddff29aaedf4f5383cc0970e9ba9d51e99e6e9027d18bd3c2f75d36857f37f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7299669$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2901039$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>SUJAY SINGH</creatorcontrib><creatorcontrib>LOWE, D. G</creatorcontrib><creatorcontrib>THORPE, D. 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We report here that the deduced amino-acid sequence of the spermatozoan membrane form of guanylate cyclase predicts an intrinsic membrane protein of 986 amino acids with an amino-terminal signal sequence. A single transmembrane domain separates the protein into putative extracellular and cytoplasmic-catalytic domains. The cytoplasmic carboxyl-terminal 95 amino acids contain 20% serine, the likely regulatory sites for phosphorylation. Unexpectedly, the enzyme is homologous to the protein kinase family.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Cell Membrane - enzymology</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>Cellular biology</subject><subject>DNA - genetics</subject><subject>DNA, Recombinant</subject><subject>Enzymatic activity</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetics</subject><subject>Glycosylation</subject><subject>Guanylate Cyclase - genetics</subject><subject>Guanylate Cyclase - isolation & purification</subject><subject>Humans</subject><subject>Male</subject><subject>Medical research</subject><subject>Membranes</subject><subject>Mice</subject><subject>Molecular and cellular biology</subject><subject>Molecular Sequence Data</subject><subject>Peptides</subject><subject>Protein Kinases</subject><subject>Proteins</subject><subject>Receptors, Cell Surface</subject><subject>Sea Urchins</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Spermatozoa - enzymology</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1LxDAQhoMo6_oB_gEhiIiX6jRpm-Qoi1-geFGvJZtMtNo2a9Ii---N7OrBizAwh3nm452XkIMcznLg8pzzQoDUsEGmeSGqrKik2CRTACYzkLzaJjsxvgFAmYtiQiZMQepTU_J8j9086B7py6j7ZasHpGZpWh2RNpFqarBtszgGpw3SgAYXgw_0sxle6avvfOtflnTwdBH8gE1P35s-tcY9suV0G3F_nXfJ09Xl4-wmu3u4vp1d3GWGV-WQWWetc0xpjdYVruSSGwNKAKq5VrbMUSmsUAETNpdzyw1zorS8kqVwPMUuOVnNTfs_RoxD3TXx--SkyI-xFpIrzpX6F-QlEyx9MYFHf8A3P4Y-iagZFEUBCsoEna4gE3yMAV29CE2nw7LOof42pP4xJKGH63njvEP7C64dSPXjdV1Ho1uXvDBN_MUEU6qqFP8CBMCSMw</recordid><startdate>19880825</startdate><enddate>19880825</enddate><creator>SUJAY SINGH</creator><creator>LOWE, D. 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Psychology</topic><topic>Genetics</topic><topic>Glycosylation</topic><topic>Guanylate Cyclase - genetics</topic><topic>Guanylate Cyclase - isolation & purification</topic><topic>Humans</topic><topic>Male</topic><topic>Medical research</topic><topic>Membranes</topic><topic>Mice</topic><topic>Molecular and cellular biology</topic><topic>Molecular Sequence Data</topic><topic>Peptides</topic><topic>Protein Kinases</topic><topic>Proteins</topic><topic>Receptors, Cell Surface</topic><topic>Sea Urchins</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Spermatozoa - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>SUJAY SINGH</creatorcontrib><creatorcontrib>LOWE, D. G</creatorcontrib><creatorcontrib>THORPE, D. S</creatorcontrib><creatorcontrib>RODRIGUEZ, H</creatorcontrib><creatorcontrib>WUN-JING KUANG</creatorcontrib><creatorcontrib>DANGOTT, L. 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| identifier | ISSN: 0028-0836 |
| ispartof | Nature (London), 1988-08, Vol.334 (6184), p.708-712 |
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| language | eng |
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| source | MEDLINE; Springer Nature - Complete Springer Journals; Nature Journals Online |
| subjects | Amino Acid Sequence Amino acids Animals Base Sequence Biological and medical sciences Cell Membrane - enzymology Cell receptors Cell structures and functions Cellular biology DNA - genetics DNA, Recombinant Enzymatic activity Fundamental and applied biological sciences. Psychology Genetics Glycosylation Guanylate Cyclase - genetics Guanylate Cyclase - isolation & purification Humans Male Medical research Membranes Mice Molecular and cellular biology Molecular Sequence Data Peptides Protein Kinases Proteins Receptors, Cell Surface Sea Urchins Sequence Homology, Nucleic Acid Spermatozoa - enzymology |
| title | Membrane guanylate cyclase is a cell-surface receptor with homology to protein kinases |
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