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Regulation of repulsion versus adhesion by different splice forms of an Eph receptor
Eph tyrosine kinase receptors and their membrane-bound ephrin ligands mediate cell interactions and participate in several developmental processes 1 , 2 , 3 , 4 . Ligand binding to an Eph receptor results in tyrosine phosphorylation of the kinase domain, and repulsion of axonal growth cones and migr...
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| Published in: | Nature (London) 2000-11, Vol.408 (6809), p.203-206 |
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| cites | cdi_FETCH-LOGICAL-c642t-8f4abcabd5b651ea34a8467ec534cd3aa8db63efa5adc12b864f3720d887866c3 |
| container_end_page | 206 |
| container_issue | 6809 |
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| container_title | Nature (London) |
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| creator | Holmberg, Johan Clarke, Diana L. Frisén, Jonas |
| description | Eph tyrosine kinase receptors and their membrane-bound ephrin ligands mediate cell interactions and participate in several developmental processes
1
,
2
,
3
,
4
. Ligand binding to an Eph receptor results in tyrosine phosphorylation of the kinase domain, and repulsion of axonal growth cones and migrating cells. Here we report that a subpopulation of ephrin-A5 null mice display neural tube defects resembling anencephaly in man. This is caused by the failure of the neural folds to fuse in the dorsal midline, suggesting that ephrin-A5, in addition to its involvement in cell repulsion
5
,
6
, can participate in cell adhesion. During neurulation, ephrin-A5 is co-expressed with its cognate receptor EphA7 in cells at the edges of the dorsal neural folds. Three different EphA7 splice variants
7
,
8
, a full-length form and two truncated versions lacking kinase domains, are expressed in the neural folds. Co-expression of an endogenously expressed truncated form of EphA7 suppresses tyrosine phosphorylation of the full-length EphA7 receptor and shifts the cellular response from repulsion to adhesion
in vitro
. We conclude that alternative usage of different splice forms of a tyrosine kinase receptor can mediate cellular adhesion or repulsion during embryonic development. |
| doi_str_mv | 10.1038/35041577 |
| format | article |
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1
,
2
,
3
,
4
. Ligand binding to an Eph receptor results in tyrosine phosphorylation of the kinase domain, and repulsion of axonal growth cones and migrating cells. Here we report that a subpopulation of ephrin-A5 null mice display neural tube defects resembling anencephaly in man. This is caused by the failure of the neural folds to fuse in the dorsal midline, suggesting that ephrin-A5, in addition to its involvement in cell repulsion
5
,
6
, can participate in cell adhesion. During neurulation, ephrin-A5 is co-expressed with its cognate receptor EphA7 in cells at the edges of the dorsal neural folds. Three different EphA7 splice variants
7
,
8
, a full-length form and two truncated versions lacking kinase domains, are expressed in the neural folds. Co-expression of an endogenously expressed truncated form of EphA7 suppresses tyrosine phosphorylation of the full-length EphA7 receptor and shifts the cellular response from repulsion to adhesion
in vitro
. We conclude that alternative usage of different splice forms of a tyrosine kinase receptor can mediate cellular adhesion or repulsion during embryonic development.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/35041577</identifier><identifier>PMID: 11089974</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Abnormalities ; Adhesion ; Alternative Splicing ; Animals ; Biological and medical sciences ; Cell adhesion ; Cell Adhesion - physiology ; Cell Line ; Cell physiology ; Cell receptors ; Cells ; Development. Senescence. Regeneration. Transplantation ; Embryonic and Fetal Development - physiology ; Embryonic growth stage ; Embryos ; Ephrin-A5 ; Ephrins ; Female ; Fundamental and applied biological sciences. Psychology ; Humanities and Social Sciences ; letter ; Male ; Membrane Proteins - chemistry ; Membrane Proteins - genetics ; Membrane Proteins - physiology ; Membranes ; Mice ; Miscellaneous ; Molecular and cellular biology ; multidisciplinary ; Mutation ; Nervous System - embryology ; Neural tube ; Neural Tube Defects - etiology ; Neural Tube Defects - genetics ; Neurology ; Neurons - cytology ; Phosphorylation ; Physiological aspects ; Receptor Protein-Tyrosine Kinases - chemistry ; Receptor Protein-Tyrosine Kinases - genetics ; Receptor Protein-Tyrosine Kinases - physiology ; Receptor, EphA7 ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Rodents ; Science ; Science (multidisciplinary) ; Signal Transduction ; Vertebrates: nervous system and sense organs</subject><ispartof>Nature (London), 2000-11, Vol.408 (6809), p.203-206</ispartof><rights>Macmillan Magazines Ltd. 2000</rights><rights>2001 INIST-CNRS</rights><rights>COPYRIGHT 2000 Nature Publishing Group</rights><rights>Copyright Macmillan Journals Ltd. Nov 9, 2000</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c642t-8f4abcabd5b651ea34a8467ec534cd3aa8db63efa5adc12b864f3720d887866c3</citedby><cites>FETCH-LOGICAL-c642t-8f4abcabd5b651ea34a8467ec534cd3aa8db63efa5adc12b864f3720d887866c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=810958$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11089974$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttp://kipublications.ki.se/Default.aspx?queryparsed=id:1933301$$DView record from Swedish Publication Index$$Hfree_for_read</backlink></links><search><creatorcontrib>Holmberg, Johan</creatorcontrib><creatorcontrib>Clarke, Diana L.</creatorcontrib><creatorcontrib>Frisén, Jonas</creatorcontrib><title>Regulation of repulsion versus adhesion by different splice forms of an Eph receptor</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>Eph tyrosine kinase receptors and their membrane-bound ephrin ligands mediate cell interactions and participate in several developmental processes
1
,
2
,
3
,
4
. Ligand binding to an Eph receptor results in tyrosine phosphorylation of the kinase domain, and repulsion of axonal growth cones and migrating cells. Here we report that a subpopulation of ephrin-A5 null mice display neural tube defects resembling anencephaly in man. This is caused by the failure of the neural folds to fuse in the dorsal midline, suggesting that ephrin-A5, in addition to its involvement in cell repulsion
5
,
6
, can participate in cell adhesion. During neurulation, ephrin-A5 is co-expressed with its cognate receptor EphA7 in cells at the edges of the dorsal neural folds. Three different EphA7 splice variants
7
,
8
, a full-length form and two truncated versions lacking kinase domains, are expressed in the neural folds. Co-expression of an endogenously expressed truncated form of EphA7 suppresses tyrosine phosphorylation of the full-length EphA7 receptor and shifts the cellular response from repulsion to adhesion
in vitro
. We conclude that alternative usage of different splice forms of a tyrosine kinase receptor can mediate cellular adhesion or repulsion during embryonic development.</description><subject>Abnormalities</subject><subject>Adhesion</subject><subject>Alternative Splicing</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cell adhesion</subject><subject>Cell Adhesion - physiology</subject><subject>Cell Line</subject><subject>Cell physiology</subject><subject>Cell receptors</subject><subject>Cells</subject><subject>Development. Senescence. Regeneration. Transplantation</subject><subject>Embryonic and Fetal Development - physiology</subject><subject>Embryonic growth stage</subject><subject>Embryos</subject><subject>Ephrin-A5</subject><subject>Ephrins</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humanities and Social Sciences</subject><subject>letter</subject><subject>Male</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - physiology</subject><subject>Membranes</subject><subject>Mice</subject><subject>Miscellaneous</subject><subject>Molecular and cellular biology</subject><subject>multidisciplinary</subject><subject>Mutation</subject><subject>Nervous System - embryology</subject><subject>Neural tube</subject><subject>Neural Tube Defects - etiology</subject><subject>Neural Tube Defects - genetics</subject><subject>Neurology</subject><subject>Neurons - cytology</subject><subject>Phosphorylation</subject><subject>Physiological aspects</subject><subject>Receptor Protein-Tyrosine Kinases - chemistry</subject><subject>Receptor Protein-Tyrosine Kinases - genetics</subject><subject>Receptor Protein-Tyrosine Kinases - physiology</subject><subject>Receptor, EphA7</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Rodents</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Signal Transduction</subject><subject>Vertebrates: nervous system and sense organs</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><recordid>eNp90s1u1DAQAOAIgehSkHgCFFGJn0OK7Ti2c6yqQitVQirlbE2c8dYlG6d2AvTt8bJpl4UK5ZDY-WY8mUyWvaTkkJJSfSgrwmkl5aNsQbkUBRdKPs4WhDBVEFWKvexZjNeEkIpK_jTbo5SoupZ8kV1e4HLqYHS-z73NAw5TF9eL7xjiFHNor_D3urnNW2ctBuzHPA6dM5hbH1ZxHQZ9fjJcpWiDw-jD8-yJhS7ii_m-n339eHJ5fFqcf_50dnx0XhjB2Vgoy6Ex0LRVIyqKUHJQXEg0VclNWwKothElWqigNZQ1SnBbSkZapaQSwpT7WbHJG3-kuhs9BLeCcKs9OD1vfUtPqKu6rhlP_u3GD8HfTBhHvXLRYNdBj36KWvKSU0EES_LN_yXjjHMmE3z9F7z2U-jTV2tGOJec1HJb5xI61K63fgxglthjgM73aF3aPmJUVSz9FbJNuuPN4G70n-jwAZSuFlfOPJj1_U5AMiP-HJcwxajPvlzs2ncba4KPMaC97y0lej1y-m7kEn01d2BqVthu4TxjCRzMAKKBzgbojYv3TlFSV2pbXUwv-iWGbSP_OfIX8GjnMg</recordid><startdate>20001109</startdate><enddate>20001109</enddate><creator>Holmberg, Johan</creator><creator>Clarke, Diana L.</creator><creator>Frisén, Jonas</creator><general>Nature Publishing Group UK</general><general>Nature Publishing</general><general>Nature Publishing Group</general><scope>IQODW</scope><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>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7ST</scope><scope>7T5</scope><scope>7TG</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88G</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2M</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PSYQQ</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>R05</scope><scope>RC3</scope><scope>S0X</scope><scope>SOI</scope><scope>7X8</scope><scope>7SC</scope><scope>7SP</scope><scope>7SR</scope><scope>7TB</scope><scope>7U5</scope><scope>8BQ</scope><scope>F28</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>ADTPV</scope><scope>AOWAS</scope></search><sort><creationdate>20001109</creationdate><title>Regulation of repulsion versus adhesion by different splice forms of an Eph receptor</title><author>Holmberg, Johan ; Clarke, Diana L. ; Frisén, Jonas</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c642t-8f4abcabd5b651ea34a8467ec534cd3aa8db63efa5adc12b864f3720d887866c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Abnormalities</topic><topic>Adhesion</topic><topic>Alternative Splicing</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cell adhesion</topic><topic>Cell Adhesion - physiology</topic><topic>Cell Line</topic><topic>Cell physiology</topic><topic>Cell receptors</topic><topic>Cells</topic><topic>Development. Senescence. Regeneration. Transplantation</topic><topic>Embryonic and Fetal Development - physiology</topic><topic>Embryonic growth stage</topic><topic>Embryos</topic><topic>Ephrin-A5</topic><topic>Ephrins</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humanities and Social Sciences</topic><topic>letter</topic><topic>Male</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - physiology</topic><topic>Membranes</topic><topic>Mice</topic><topic>Miscellaneous</topic><topic>Molecular and cellular biology</topic><topic>multidisciplinary</topic><topic>Mutation</topic><topic>Nervous System - embryology</topic><topic>Neural tube</topic><topic>Neural Tube Defects - etiology</topic><topic>Neural Tube Defects - genetics</topic><topic>Neurology</topic><topic>Neurons - cytology</topic><topic>Phosphorylation</topic><topic>Physiological aspects</topic><topic>Receptor Protein-Tyrosine Kinases - chemistry</topic><topic>Receptor Protein-Tyrosine Kinases - genetics</topic><topic>Receptor Protein-Tyrosine Kinases - physiology</topic><topic>Receptor, EphA7</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Rodents</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>Signal Transduction</topic><topic>Vertebrates: nervous system and sense organs</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Holmberg, Johan</creatorcontrib><creatorcontrib>Clarke, Diana L.</creatorcontrib><creatorcontrib>Frisén, Jonas</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>ProQuest Nursing and Allied Health Source</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Environment Abstracts</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical 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>Agricultural Science Collection</collection><collection>ProQuest_Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Psychology Database (Alumni)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central</collection><collection>Advanced Technologies & Aerospace Database (1962 - 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1
,
2
,
3
,
4
. Ligand binding to an Eph receptor results in tyrosine phosphorylation of the kinase domain, and repulsion of axonal growth cones and migrating cells. Here we report that a subpopulation of ephrin-A5 null mice display neural tube defects resembling anencephaly in man. This is caused by the failure of the neural folds to fuse in the dorsal midline, suggesting that ephrin-A5, in addition to its involvement in cell repulsion
5
,
6
, can participate in cell adhesion. During neurulation, ephrin-A5 is co-expressed with its cognate receptor EphA7 in cells at the edges of the dorsal neural folds. Three different EphA7 splice variants
7
,
8
, a full-length form and two truncated versions lacking kinase domains, are expressed in the neural folds. Co-expression of an endogenously expressed truncated form of EphA7 suppresses tyrosine phosphorylation of the full-length EphA7 receptor and shifts the cellular response from repulsion to adhesion
in vitro
. We conclude that alternative usage of different splice forms of a tyrosine kinase receptor can mediate cellular adhesion or repulsion during embryonic development.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>11089974</pmid><doi>10.1038/35041577</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0028-0836 |
| ispartof | Nature (London), 2000-11, Vol.408 (6809), p.203-206 |
| issn | 0028-0836 1476-4687 |
| language | eng |
| recordid | cdi_swepub_primary_oai_swepub_ki_se_599924 |
| source | Springer Nature - Connect here FIRST to enable access |
| subjects | Abnormalities Adhesion Alternative Splicing Animals Biological and medical sciences Cell adhesion Cell Adhesion - physiology Cell Line Cell physiology Cell receptors Cells Development. Senescence. Regeneration. Transplantation Embryonic and Fetal Development - physiology Embryonic growth stage Embryos Ephrin-A5 Ephrins Female Fundamental and applied biological sciences. Psychology Humanities and Social Sciences letter Male Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - physiology Membranes Mice Miscellaneous Molecular and cellular biology multidisciplinary Mutation Nervous System - embryology Neural tube Neural Tube Defects - etiology Neural Tube Defects - genetics Neurology Neurons - cytology Phosphorylation Physiological aspects Receptor Protein-Tyrosine Kinases - chemistry Receptor Protein-Tyrosine Kinases - genetics Receptor Protein-Tyrosine Kinases - physiology Receptor, EphA7 Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Rodents Science Science (multidisciplinary) Signal Transduction Vertebrates: nervous system and sense organs |
| title | Regulation of repulsion versus adhesion by different splice forms of an Eph receptor |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-21T09%3A38%3A30IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_swepu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Regulation%20of%20repulsion%20versus%20adhesion%20by%20different%20splice%20forms%20of%20an%20Eph%20receptor&rft.jtitle=Nature%20(London)&rft.au=Holmberg,%20Johan&rft.date=2000-11-09&rft.volume=408&rft.issue=6809&rft.spage=203&rft.epage=206&rft.pages=203-206&rft.issn=0028-0836&rft.eissn=1476-4687&rft.coden=NATUAS&rft_id=info:doi/10.1038/35041577&rft_dat=%3Cgale_swepu%3EA218529970%3C/gale_swepu%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c642t-8f4abcabd5b651ea34a8467ec534cd3aa8db63efa5adc12b864f3720d887866c3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=204474097&rft_id=info:pmid/11089974&rft_galeid=A218529970&rfr_iscdi=true |