The C9orf72 GGGGCC Repeat Is Translated into Aggregating Dipeptide-Repeat Proteins in FTLD/ALS
Expansion of a GGGGCC hexanucleotide repeat upstream of the C9orf72 coding region is the most common cause of familial frontotemporal lobar degeneration and amyotrophic lateral sclerosis (FTLD/ALS), but the pathomechanisms involved are unknown. As in other FTLD/ALS variants, characteristic intracell...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2013-03, Vol.339 (6125), p.1335-1338 |
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| creator | Mori, Kohji Weng, Shih-Ming Arzberger, Thomas May, Stephanie Rentzsch, Kristin Kremmer, Elisabeth Schmid, Bettina Kretzschmar, Hans A. Cruts, Marc Van Broeckhoven, Christine Haass, Christian Edbauer, Dieter |
| description | Expansion of a GGGGCC hexanucleotide repeat upstream of the C9orf72 coding region is the most common cause of familial frontotemporal lobar degeneration and amyotrophic lateral sclerosis (FTLD/ALS), but the pathomechanisms involved are unknown. As in other FTLD/ALS variants, characteristic intracellular inclusions of misfolded proteins define C9orf72 pathology, but the core proteins of the majority of inclusions are still unknown. Here, we found that most of these characteristic inclusions contain poly-(Gly-Ala) and, to a lesser extent, poly-(Gly-Pro) and poly-(Gly-Arg) dipeptide-repeat proteins presumably generated by non-ATG—initiated translation from the expanded GGGGCC repeat in three reading frames. These findings directly link the FTLD/ALS-associated genetic mutation to the predominant pathology in patients with C9orf72 hexanucleotide expansion. |
| doi_str_mv | 10.1126/science.1232927 |
| format | Article |
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As in other FTLD/ALS variants, characteristic intracellular inclusions of misfolded proteins define C9orf72 pathology, but the core proteins of the majority of inclusions are still unknown. Here, we found that most of these characteristic inclusions contain poly-(Gly-Ala) and, to a lesser extent, poly-(Gly-Pro) and poly-(Gly-Arg) dipeptide-repeat proteins presumably generated by non-ATG—initiated translation from the expanded GGGGCC repeat in three reading frames. These findings directly link the FTLD/ALS-associated genetic mutation to the predominant pathology in patients with C9orf72 hexanucleotide expansion.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.1232927</identifier><identifier>PMID: 23393093</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>United States: American Association for the Advancement of Science</publisher><subject>Adaptor Proteins, Signal Transducing - metabolism ; Amyotrophic lateral sclerosis ; Amyotrophic Lateral Sclerosis - genetics ; Amyotrophic Lateral Sclerosis - metabolism ; Amyotrophic Lateral Sclerosis - pathology ; Anatomy ; Antibodies ; C9orf72 Protein ; Central nervous system ; Cerebellum ; Cerebellum - metabolism ; Cerebellum - pathology ; Coding ; Cytoplasmic inclusions ; Dementia ; DNA Repeat Expansion ; DNA-Binding Proteins - metabolism ; Frontotemporal lobar degeneration ; Frontotemporal Lobar Degeneration - genetics ; Frontotemporal Lobar Degeneration - metabolism ; Frontotemporal Lobar Degeneration - pathology ; Genetic mutation ; Genetics ; Heterozygote ; Hippocampus ; Hippocampus - metabolism ; Hippocampus - pathology ; Humans ; Immunoblotting ; Inclusions ; Links ; Neurodegeneration ; Neurodegenerative diseases ; Open Reading Frames ; Pathology ; Patients ; Protein Biosynthesis ; Proteins ; Proteins - genetics ; Proteins - metabolism ; Sequestosome-1 Protein ; Translation ; Trucks</subject><ispartof>Science (American Association for the Advancement of Science), 2013-03, Vol.339 (6125), p.1335-1338</ispartof><rights>Copyright © 2013 American Association for the Advancement of Science</rights><rights>Copyright © 2013, American Association for the Advancement of Science</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c421t-7c60b35e11f450ce7cafceaf35398f67b136959b3cd092e9e7d5dc59cac38b803</citedby><cites>FETCH-LOGICAL-c421t-7c60b35e11f450ce7cafceaf35398f67b136959b3cd092e9e7d5dc59cac38b803</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/23380011$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/23380011$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,776,780,799,2871,2872,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23393093$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mori, Kohji</creatorcontrib><creatorcontrib>Weng, Shih-Ming</creatorcontrib><creatorcontrib>Arzberger, Thomas</creatorcontrib><creatorcontrib>May, Stephanie</creatorcontrib><creatorcontrib>Rentzsch, Kristin</creatorcontrib><creatorcontrib>Kremmer, Elisabeth</creatorcontrib><creatorcontrib>Schmid, Bettina</creatorcontrib><creatorcontrib>Kretzschmar, Hans A.</creatorcontrib><creatorcontrib>Cruts, Marc</creatorcontrib><creatorcontrib>Van Broeckhoven, Christine</creatorcontrib><creatorcontrib>Haass, Christian</creatorcontrib><creatorcontrib>Edbauer, Dieter</creatorcontrib><title>The C9orf72 GGGGCC Repeat Is Translated into Aggregating Dipeptide-Repeat Proteins in FTLD/ALS</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>Expansion of a GGGGCC hexanucleotide repeat upstream of the C9orf72 coding region is the most common cause of familial frontotemporal lobar degeneration and amyotrophic lateral sclerosis (FTLD/ALS), but the pathomechanisms involved are unknown. As in other FTLD/ALS variants, characteristic intracellular inclusions of misfolded proteins define C9orf72 pathology, but the core proteins of the majority of inclusions are still unknown. Here, we found that most of these characteristic inclusions contain poly-(Gly-Ala) and, to a lesser extent, poly-(Gly-Pro) and poly-(Gly-Arg) dipeptide-repeat proteins presumably generated by non-ATG—initiated translation from the expanded GGGGCC repeat in three reading frames. These findings directly link the FTLD/ALS-associated genetic mutation to the predominant pathology in patients with C9orf72 hexanucleotide expansion.</description><subject>Adaptor Proteins, Signal Transducing - metabolism</subject><subject>Amyotrophic lateral sclerosis</subject><subject>Amyotrophic Lateral Sclerosis - genetics</subject><subject>Amyotrophic Lateral Sclerosis - metabolism</subject><subject>Amyotrophic Lateral Sclerosis - pathology</subject><subject>Anatomy</subject><subject>Antibodies</subject><subject>C9orf72 Protein</subject><subject>Central nervous system</subject><subject>Cerebellum</subject><subject>Cerebellum - metabolism</subject><subject>Cerebellum - pathology</subject><subject>Coding</subject><subject>Cytoplasmic inclusions</subject><subject>Dementia</subject><subject>DNA Repeat Expansion</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Frontotemporal lobar degeneration</subject><subject>Frontotemporal Lobar Degeneration - genetics</subject><subject>Frontotemporal Lobar Degeneration - metabolism</subject><subject>Frontotemporal Lobar Degeneration - pathology</subject><subject>Genetic mutation</subject><subject>Genetics</subject><subject>Heterozygote</subject><subject>Hippocampus</subject><subject>Hippocampus - metabolism</subject><subject>Hippocampus - pathology</subject><subject>Humans</subject><subject>Immunoblotting</subject><subject>Inclusions</subject><subject>Links</subject><subject>Neurodegeneration</subject><subject>Neurodegenerative diseases</subject><subject>Open Reading Frames</subject><subject>Pathology</subject><subject>Patients</subject><subject>Protein Biosynthesis</subject><subject>Proteins</subject><subject>Proteins - genetics</subject><subject>Proteins - metabolism</subject><subject>Sequestosome-1 Protein</subject><subject>Translation</subject><subject>Trucks</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0bFu2zAQBmAiSJG4aedMCQhk6aL4yLNEcjSUJg1goEXrrhUo6uTIsCWFpIe-fWlYLYouveWG-3g44mfsWsC9ELKYB9dR7-heSJRGqjM2E2DyzEjAczYDwCLToPJL9jaELUCaGbxglxLRIBicsR_rF-KlGXyrJH9KVZb8K41kI38OfO1tH3Y2UsO7Pg58udl42tjY9Rv-0I00xq6hbPJf_BCp60Oi_HG9epgvV9_esTet3QV6P_Ur9v3x47r8lK0-Pz2Xy1XmFlLETLkCasxJiHaRgyPlbOvItpij0W2haoFFOr1G14CRZEg1eeNy46xDXWvAK_bhtHf0w-uBQqz2XXC029mehkOohAYt5MLI4v8UhdKoDMhE7_6h2-Hg-_SRoyq0OVZS85NyfgjBU1uNvttb_7MSUB1TqqaUqiml9OJ22nuo99T88b9jSeDmBLYhDv7vuQYQAn8BofuVTQ</recordid><startdate>20130315</startdate><enddate>20130315</enddate><creator>Mori, Kohji</creator><creator>Weng, Shih-Ming</creator><creator>Arzberger, Thomas</creator><creator>May, Stephanie</creator><creator>Rentzsch, Kristin</creator><creator>Kremmer, Elisabeth</creator><creator>Schmid, Bettina</creator><creator>Kretzschmar, Hans A.</creator><creator>Cruts, Marc</creator><creator>Van Broeckhoven, Christine</creator><creator>Haass, Christian</creator><creator>Edbauer, Dieter</creator><general>American Association for the Advancement of Science</general><general>The American Association for the Advancement of Science</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>7QF</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7SS</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TK</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>K9.</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20130315</creationdate><title>The C9orf72 GGGGCC Repeat Is Translated into Aggregating Dipeptide-Repeat Proteins in FTLD/ALS</title><author>Mori, Kohji ; Weng, Shih-Ming ; Arzberger, Thomas ; May, Stephanie ; Rentzsch, Kristin ; Kremmer, Elisabeth ; Schmid, Bettina ; Kretzschmar, Hans A. ; Cruts, Marc ; Van Broeckhoven, Christine ; Haass, Christian ; Edbauer, Dieter</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c421t-7c60b35e11f450ce7cafceaf35398f67b136959b3cd092e9e7d5dc59cac38b803</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Adaptor Proteins, Signal Transducing - 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Academic</collection><jtitle>Science (American Association for the Advancement of Science)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mori, Kohji</au><au>Weng, Shih-Ming</au><au>Arzberger, Thomas</au><au>May, Stephanie</au><au>Rentzsch, Kristin</au><au>Kremmer, Elisabeth</au><au>Schmid, Bettina</au><au>Kretzschmar, Hans A.</au><au>Cruts, Marc</au><au>Van Broeckhoven, Christine</au><au>Haass, Christian</au><au>Edbauer, Dieter</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The C9orf72 GGGGCC Repeat Is Translated into Aggregating Dipeptide-Repeat Proteins in FTLD/ALS</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>2013-03-15</date><risdate>2013</risdate><volume>339</volume><issue>6125</issue><spage>1335</spage><epage>1338</epage><pages>1335-1338</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>Expansion of a GGGGCC hexanucleotide repeat upstream of the C9orf72 coding region is the most common cause of familial frontotemporal lobar degeneration and amyotrophic lateral sclerosis (FTLD/ALS), but the pathomechanisms involved are unknown. As in other FTLD/ALS variants, characteristic intracellular inclusions of misfolded proteins define C9orf72 pathology, but the core proteins of the majority of inclusions are still unknown. Here, we found that most of these characteristic inclusions contain poly-(Gly-Ala) and, to a lesser extent, poly-(Gly-Pro) and poly-(Gly-Arg) dipeptide-repeat proteins presumably generated by non-ATG—initiated translation from the expanded GGGGCC repeat in three reading frames. These findings directly link the FTLD/ALS-associated genetic mutation to the predominant pathology in patients with C9orf72 hexanucleotide expansion.</abstract><cop>United States</cop><pub>American Association for the Advancement of Science</pub><pmid>23393093</pmid><doi>10.1126/science.1232927</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| source | American Association for the Advancement of Science; Jstor Complete Legacy; MEDLINE |
| subjects | Adaptor Proteins, Signal Transducing - metabolism Amyotrophic lateral sclerosis Amyotrophic Lateral Sclerosis - genetics Amyotrophic Lateral Sclerosis - metabolism Amyotrophic Lateral Sclerosis - pathology Anatomy Antibodies C9orf72 Protein Central nervous system Cerebellum Cerebellum - metabolism Cerebellum - pathology Coding Cytoplasmic inclusions Dementia DNA Repeat Expansion DNA-Binding Proteins - metabolism Frontotemporal lobar degeneration Frontotemporal Lobar Degeneration - genetics Frontotemporal Lobar Degeneration - metabolism Frontotemporal Lobar Degeneration - pathology Genetic mutation Genetics Heterozygote Hippocampus Hippocampus - metabolism Hippocampus - pathology Humans Immunoblotting Inclusions Links Neurodegeneration Neurodegenerative diseases Open Reading Frames Pathology Patients Protein Biosynthesis Proteins Proteins - genetics Proteins - metabolism Sequestosome-1 Protein Translation Trucks |
| title | The C9orf72 GGGGCC Repeat Is Translated into Aggregating Dipeptide-Repeat Proteins in FTLD/ALS |
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