The epilepsy gene LGI1 encodes a secreted glycoprotein that binds to the cell surface
Autosomal dominant lateral temporal epilepsy (ADTLE) is a partial epilepsy caused by mutations in LGI1, a multidomain protein of unknown function. To begin to understand the biological function of LGI1, we have determined its pattern of glycosylation, subcellular expression and capacity for secretio...
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| Veröffentlicht in: | Human molecular genetics 2006-12, Vol.15 (23), p.3436-3445 |
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| creator | Sirerol-Piquer, Maria Salomé Ayerdi-Izquierdo, Ana Morante-Redolat, José Manuel Herranz-Pérez, Vicente Favell, Kristy Barker, Philip A. Pérez-Tur, Jordi |
| description | Autosomal dominant lateral temporal epilepsy (ADTLE) is a partial epilepsy caused by mutations in LGI1, a multidomain protein of unknown function. To begin to understand the biological function of LGI1, we have determined its pattern of glycosylation, subcellular expression and capacity for secretion. LGI1 is expressed as two different isoforms in the brain, and we show that the long isoform is a secreted protein, whereas the short isoform is retained in an intracellular pool. ADLTE-related mutants of the long form are defective for secretion and are retained in the endoplasmic reticulum and Golgi complex. Finally, we show that normal secreted LGI1 specifically binds to the cell surface of differentiated PC12 cells. We propose that LGI1 is a secreted factor important for neuronal development and that ADTLE is a disease that results from the loss of regulation in the protein available either extracellular or intracellularly. |
| doi_str_mv | 10.1093/hmg/ddl421 |
| format | Article |
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To begin to understand the biological function of LGI1, we have determined its pattern of glycosylation, subcellular expression and capacity for secretion. LGI1 is expressed as two different isoforms in the brain, and we show that the long isoform is a secreted protein, whereas the short isoform is retained in an intracellular pool. ADLTE-related mutants of the long form are defective for secretion and are retained in the endoplasmic reticulum and Golgi complex. Finally, we show that normal secreted LGI1 specifically binds to the cell surface of differentiated PC12 cells. We propose that LGI1 is a secreted factor important for neuronal development and that ADTLE is a disease that results from the loss of regulation in the protein available either extracellular or intracellularly.</description><identifier>ISSN: 0964-6906</identifier><identifier>EISSN: 1460-2083</identifier><identifier>DOI: 10.1093/hmg/ddl421</identifier><identifier>PMID: 17067999</identifier><identifier>CODEN: HNGEE5</identifier><language>eng</language><publisher>Oxford: Oxford University Press</publisher><subject>Animals ; Biological and medical sciences ; Cell Membrane - chemistry ; Cells, Cultured ; Enzyme Activation ; Epilepsy, Temporal Lobe - genetics ; Fundamental and applied biological sciences. Psychology ; Genetics of eukaryotes. Biological and molecular evolution ; Glycoproteins - analysis ; Glycoproteins - genetics ; Glycoproteins - metabolism ; Glycosylation ; Headache. Facial pains. Syncopes. Epilepsia. Intracranial hypertension. Brain oedema. Cerebral palsy ; Humans ; Medical sciences ; Mitogen-Activated Protein Kinase 1 - metabolism ; Mitogen-Activated Protein Kinase 3 - metabolism ; Molecular and cellular biology ; Nervous system (semeiology, syndromes) ; Neurology ; PC12 Cells ; Protein Isoforms - analysis ; Protein Isoforms - genetics ; Protein Isoforms - metabolism ; Protein Structure, Tertiary - genetics ; Protein Structure, Tertiary - physiology ; Proteins - analysis ; Proteins - genetics ; Proteins - metabolism ; Rats</subject><ispartof>Human molecular genetics, 2006-12, Vol.15 (23), p.3436-3445</ispartof><rights>2007 INIST-CNRS</rights><rights>Copyright Oxford University Press(England) Dec 1, 2006</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c447t-d3aa9ea82f1374b337fe8c6f0f9827fab48d422d591df621d3326b27896cde803</citedby><cites>FETCH-LOGICAL-c447t-d3aa9ea82f1374b337fe8c6f0f9827fab48d422d591df621d3326b27896cde803</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18355610$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17067999$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sirerol-Piquer, Maria Salomé</creatorcontrib><creatorcontrib>Ayerdi-Izquierdo, Ana</creatorcontrib><creatorcontrib>Morante-Redolat, José Manuel</creatorcontrib><creatorcontrib>Herranz-Pérez, Vicente</creatorcontrib><creatorcontrib>Favell, Kristy</creatorcontrib><creatorcontrib>Barker, Philip A.</creatorcontrib><creatorcontrib>Pérez-Tur, Jordi</creatorcontrib><title>The epilepsy gene LGI1 encodes a secreted glycoprotein that binds to the cell surface</title><title>Human molecular genetics</title><addtitle>Hum Mol Genet</addtitle><description>Autosomal dominant lateral temporal epilepsy (ADTLE) is a partial epilepsy caused by mutations in LGI1, a multidomain protein of unknown function. To begin to understand the biological function of LGI1, we have determined its pattern of glycosylation, subcellular expression and capacity for secretion. LGI1 is expressed as two different isoforms in the brain, and we show that the long isoform is a secreted protein, whereas the short isoform is retained in an intracellular pool. ADLTE-related mutants of the long form are defective for secretion and are retained in the endoplasmic reticulum and Golgi complex. Finally, we show that normal secreted LGI1 specifically binds to the cell surface of differentiated PC12 cells. We propose that LGI1 is a secreted factor important for neuronal development and that ADTLE is a disease that results from the loss of regulation in the protein available either extracellular or intracellularly.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cell Membrane - chemistry</subject><subject>Cells, Cultured</subject><subject>Enzyme Activation</subject><subject>Epilepsy, Temporal Lobe - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetics of eukaryotes. Biological and molecular evolution</subject><subject>Glycoproteins - analysis</subject><subject>Glycoproteins - genetics</subject><subject>Glycoproteins - metabolism</subject><subject>Glycosylation</subject><subject>Headache. Facial pains. Syncopes. Epilepsia. Intracranial hypertension. Brain oedema. Cerebral palsy</subject><subject>Humans</subject><subject>Medical sciences</subject><subject>Mitogen-Activated Protein Kinase 1 - metabolism</subject><subject>Mitogen-Activated Protein Kinase 3 - metabolism</subject><subject>Molecular and cellular biology</subject><subject>Nervous system (semeiology, syndromes)</subject><subject>Neurology</subject><subject>PC12 Cells</subject><subject>Protein Isoforms - analysis</subject><subject>Protein Isoforms - genetics</subject><subject>Protein Isoforms - metabolism</subject><subject>Protein Structure, Tertiary - genetics</subject><subject>Protein Structure, Tertiary - physiology</subject><subject>Proteins - analysis</subject><subject>Proteins - genetics</subject><subject>Proteins - metabolism</subject><subject>Rats</subject><issn>0964-6906</issn><issn>1460-2083</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0U2LFDEQBuAgijuuXvwBEgQ9CO2mknQ-juuiOyujXnZBvIR0Upnptad7TLrB-ff2MIMLXjwVRT0UVbyEvAT2HpgVF5vt-iLGTnJ4RBYgFas4M-IxWTCrZKUsU2fkWSn3jIGSQj8lZ6CZ0tbaBbm73SDFXdvhruzpGnukq-sboNiHIWKhnhYMGUeMdN3tw7DLw4htT8eNH2nT9rHQcZg7pAG7jpYpJx_wOXmSfFfwxamek7tPH2-vltXq2_XN1eWqClLqsYrCe4ve8ARCy0YIndAElViyhuvkG2mi5DzWFmJSHKIQXDVcG6tCRMPEOXl73Duf9WvCMrptWw6H-B6HqThlQHEr9X8hWGmVsXaGr_-B98OU-_kJxwEEKCZgRu-OKOShlIzJ7XK79XnvgLlDJG6OxB0jmfGr08ap2WJ8oKcMZvDmBHwJvkvZ96EtD86IulZweLY6uraM-Pvv3OefTmmha7f8_sPVS8u_fP38wS3FH1c1omY</recordid><startdate>20061201</startdate><enddate>20061201</enddate><creator>Sirerol-Piquer, Maria Salomé</creator><creator>Ayerdi-Izquierdo, Ana</creator><creator>Morante-Redolat, José Manuel</creator><creator>Herranz-Pérez, Vicente</creator><creator>Favell, Kristy</creator><creator>Barker, Philip A.</creator><creator>Pérez-Tur, Jordi</creator><general>Oxford University Press</general><general>Oxford Publishing Limited (England)</general><scope>BSCLL</scope><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>7QP</scope><scope>7TK</scope><scope>8FD</scope><scope>FR3</scope><scope>K9.</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20061201</creationdate><title>The epilepsy gene LGI1 encodes a secreted glycoprotein that binds to the cell surface</title><author>Sirerol-Piquer, Maria Salomé ; Ayerdi-Izquierdo, Ana ; Morante-Redolat, José Manuel ; Herranz-Pérez, Vicente ; Favell, Kristy ; Barker, Philip A. ; Pérez-Tur, Jordi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c447t-d3aa9ea82f1374b337fe8c6f0f9827fab48d422d591df621d3326b27896cde803</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cell Membrane - chemistry</topic><topic>Cells, Cultured</topic><topic>Enzyme Activation</topic><topic>Epilepsy, Temporal Lobe - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genetics of eukaryotes. Biological and molecular evolution</topic><topic>Glycoproteins - analysis</topic><topic>Glycoproteins - genetics</topic><topic>Glycoproteins - metabolism</topic><topic>Glycosylation</topic><topic>Headache. Facial pains. Syncopes. Epilepsia. Intracranial hypertension. Brain oedema. Cerebral palsy</topic><topic>Humans</topic><topic>Medical sciences</topic><topic>Mitogen-Activated Protein Kinase 1 - metabolism</topic><topic>Mitogen-Activated Protein Kinase 3 - metabolism</topic><topic>Molecular and cellular biology</topic><topic>Nervous system (semeiology, syndromes)</topic><topic>Neurology</topic><topic>PC12 Cells</topic><topic>Protein Isoforms - analysis</topic><topic>Protein Isoforms - genetics</topic><topic>Protein Isoforms - metabolism</topic><topic>Protein Structure, Tertiary - genetics</topic><topic>Protein Structure, Tertiary - physiology</topic><topic>Proteins - analysis</topic><topic>Proteins - genetics</topic><topic>Proteins - metabolism</topic><topic>Rats</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sirerol-Piquer, Maria Salomé</creatorcontrib><creatorcontrib>Ayerdi-Izquierdo, Ana</creatorcontrib><creatorcontrib>Morante-Redolat, José Manuel</creatorcontrib><creatorcontrib>Herranz-Pérez, Vicente</creatorcontrib><creatorcontrib>Favell, Kristy</creatorcontrib><creatorcontrib>Barker, Philip A.</creatorcontrib><creatorcontrib>Pérez-Tur, Jordi</creatorcontrib><collection>Istex</collection><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>Calcium & Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Human molecular genetics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sirerol-Piquer, Maria Salomé</au><au>Ayerdi-Izquierdo, Ana</au><au>Morante-Redolat, José Manuel</au><au>Herranz-Pérez, Vicente</au><au>Favell, Kristy</au><au>Barker, Philip A.</au><au>Pérez-Tur, Jordi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The epilepsy gene LGI1 encodes a secreted glycoprotein that binds to the cell surface</atitle><jtitle>Human molecular genetics</jtitle><addtitle>Hum Mol Genet</addtitle><date>2006-12-01</date><risdate>2006</risdate><volume>15</volume><issue>23</issue><spage>3436</spage><epage>3445</epage><pages>3436-3445</pages><issn>0964-6906</issn><eissn>1460-2083</eissn><coden>HNGEE5</coden><abstract>Autosomal dominant lateral temporal epilepsy (ADTLE) is a partial epilepsy caused by mutations in LGI1, a multidomain protein of unknown function. To begin to understand the biological function of LGI1, we have determined its pattern of glycosylation, subcellular expression and capacity for secretion. LGI1 is expressed as two different isoforms in the brain, and we show that the long isoform is a secreted protein, whereas the short isoform is retained in an intracellular pool. ADLTE-related mutants of the long form are defective for secretion and are retained in the endoplasmic reticulum and Golgi complex. Finally, we show that normal secreted LGI1 specifically binds to the cell surface of differentiated PC12 cells. We propose that LGI1 is a secreted factor important for neuronal development and that ADTLE is a disease that results from the loss of regulation in the protein available either extracellular or intracellularly.</abstract><cop>Oxford</cop><pub>Oxford University Press</pub><pmid>17067999</pmid><doi>10.1093/hmg/ddl421</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Oxford University Press Journals All Titles (1996-Current); EZB-FREE-00999 freely available EZB journals |
| subjects | Animals Biological and medical sciences Cell Membrane - chemistry Cells, Cultured Enzyme Activation Epilepsy, Temporal Lobe - genetics Fundamental and applied biological sciences. Psychology Genetics of eukaryotes. Biological and molecular evolution Glycoproteins - analysis Glycoproteins - genetics Glycoproteins - metabolism Glycosylation Headache. Facial pains. Syncopes. Epilepsia. Intracranial hypertension. Brain oedema. Cerebral palsy Humans Medical sciences Mitogen-Activated Protein Kinase 1 - metabolism Mitogen-Activated Protein Kinase 3 - metabolism Molecular and cellular biology Nervous system (semeiology, syndromes) Neurology PC12 Cells Protein Isoforms - analysis Protein Isoforms - genetics Protein Isoforms - metabolism Protein Structure, Tertiary - genetics Protein Structure, Tertiary - physiology Proteins - analysis Proteins - genetics Proteins - metabolism Rats |
| title | The epilepsy gene LGI1 encodes a secreted glycoprotein that binds to the cell surface |
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