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<p class="publishdate"><span property="dc:date" datatype="xsd:dateTime" content="2015-09-14T00:00:00-04:00" class="date-display-single">September 14, 2015</span></p><div class='syndicate'><h1>Nuclear Pore Problems May Lead to ALS and Dementia</h1><div class="callout callout-with-border"><h3>At a Glance</h3>
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<ul class="spaced">
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<li>Researchers identified a fundamental pathway involved in some forms of amyotrophic lateral sclerosis and frontotemporal dementia.</li>
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<li>The findings may point the way to new strategies for treating these disorders.</li>
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<source srcset="https://www.nih.gov/sites/default/files/styles/floated_media_breakpoint-large/public/news-events/research-matters/2015/20150914-pore.jpg?itok=OJt-IDEM&timestamp=1442843235 1x" media="screen and (min-width: 960px)" />
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<source srcset="https://www.nih.gov/sites/default/files/styles/floated_media_breakpoint-medium/public/news-events/research-matters/2015/20150914-pore.jpg?itok=2QsyJtiL&timestamp=1442843235 1x" media="screen and (min-width: 800px)" />
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<source srcset="https://www.nih.gov/sites/default/files/styles/floated_media_breakpoint-medium-small/public/news-events/research-matters/2015/20150914-pore.jpg?itok=FD44nW7D&timestamp=1442843235 1x" media="screen and (min-width: 600px)" />
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<source srcset="https://www.nih.gov/sites/default/files/styles/floated_media_breakpoint-small/public/news-events/research-matters/2015/20150914-pore.jpg?itok=XxfDezdg&timestamp=1442843235 1x" media="screen and (min-width: 480px)" />
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<source srcset="https://www.nih.gov/sites/default/files/styles/floated_media_breakpoint-tiny/public/news-events/research-matters/2015/20150914-pore.jpg?itok=-iaaxKS9&timestamp=1442843235 1x" media="screen and (min-width: 0)" />
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<!--[if IE 9]></video><![endif]-->
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<img src="https://www.nih.gov/sites/default/files/styles/floated_media_breakpoint-medium/public/news-events/research-matters/2015/20150914-pore.jpg?itok=2QsyJtiL&timestamp=1442843235" alt="Neurons from an ALS patient" title="Neurons from an ALS patient" />
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</picture><span class="caption">Neurons (red), created from ALS patients bearing the C9ORF72 expansion, show clumps of the RanGAP protein (yellow) on their nuclei (white). The nuclei of other cells are in blue.</span><span class="credit">Jeffrey Rothstein laboratory, Johns Hopkins Medicine.</span></div>
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</div><p>Tens of thousands of Americans are currently living with amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). Both diseases are caused by the death of neurons in the central nervous system. In ALS, this leads to movement difficulty and eventual paralysis. In FTD, it causes personality changes as well as problems with language and decision-making.</p>
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<p>Recent research has connected many inherited cases of both disorders—as well as some noninherited cases—to alterations in the <em>C9ORF72</em> gene. This gene usually has less than 20 repeats of a 6-letter DNA sequence (GGGGCC, or G<sub>4</sub>C<sub>2</sub>). Disease-causing versions are expanded, containing hundreds to even thousands of these repeats. Exactly how this expansion leads to neuron death was unknown. The overly long RNA might alter the function of RNA-binding proteins or cause cells to produce toxic proteins.</p>
|
||
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||
<p>Dr. Jeffrey Rothstein’s lab at Johns Hopkins University School of Medicine previously identified more than 400 proteins that bind particularly well to G<sub>4</sub>C<sub>2</sub> repeats. To figure out whether the RNA could interact with any of these candidates to cause cell death, his lab collaborated with Dr. Thomas Lloyd’s team at Johns Hopkins. The researchers altered neurons in the eyes of fruit flies to express 30 G<sub>4</sub>C<sub>2</sub> repeats, causing eye defects. Using these flies, the team screened mutant versions of the various candidate proteins for effects on fly eyes. The work was partially funded by NIH’s National Institute of Neurological Disorders and Stroke (NINDS) and National Cancer Institute (NCI). Results were published in <em>Nature </em>on September 3, 2015.</p>
|
||
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||
<p>The scientists found less eye deterioration in flies with an overactive version of a protein called RanGAP. RanGAP is important for transporting material between the cell’s gel-like interior (cytoplasm) and the nucleus though a structure called the nuclear pore. Increasing production of RanGAP relieved movement problems in flies with the G<sub>4</sub>C<sub>2</sub> repeats. This suggests that the <em>C9ORF72</em> mutation may cause disease by disrupting this process, called nuclear or nucleocytoplasmic transport.</p>
|
||
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||
<p>The team next examined brain tissue from ALS patients with the <em>C9ORF72</em> expansion as well as neurons grown from patients’ cells. In both, the expanded RNA bound RanGAP to form abnormal clumps outside the nucleus. Other proteins involved in nuclear transport were also stuck outside. Treating neurons with compounds that prevented the RNA from interacting with RanGAP eliminated the transport problem, suggesting potential treatment strategies.</p>
|
||
|
||
<p>In an accompanying paper in <em>Nature</em>, another NIH-funded team, led by Dr. J. Paul Taylor of St. Jude Children’s Research Hospital, used a different genetic screen to look for genes that modify the effects of 58 G<sub>4</sub>C<sub>2</sub> repeats in flies. The screen identified numerous genes that encode components of the nuclear pore and the nucleocytoplasmic transport machinery, providing strong evidence for this pathway as the mechanism of neurodegeneration.</p>
|
||
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||
<p>A third study, published in <em>Nature Neuroscience</em> by a team led by Stanford University’s Dr. Aaron Gitler, focused on the potential toxic effects of proteins produced by the expanded G<sub>4</sub>C<sub>2</sub> repeats. Experiments in yeast demonstrated toxic protein effects. Like the other studies, this approach also tied the expansions to nucleocytoplasmic transport defects.</p>
|
||
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||
<p>Taken together, these studies don’t prove whether abnormal RNA-protein binding, toxic protein products, or both are responsible for diseases caused by these G<sub>4</sub>C<sub>2</sub> repeats. The results do, however, provide important insights into the disease mechanisms and highlight potential therapeutic targets.</p>
|
||
|
||
<p>“We still don’t know every step between the <em>C9ORF72</em> mutation and cellular death in the brain,” Rothstein says. “Now we have some information about what it is doing early on to damage brain and spinal cord cells.”</p>
|
||
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<p>—by Brandon Levy and Harrison Wein, Ph.D.</p>
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</div><h2 class="label-above">Related Links</h2><ul class="spaced print-urls"><li><a href="https://www.nih.gov/news-events/nih-research-matters/new-genetic-mutations-discovered-families-als" target="_top">New Genetic Mutations Discovered in Families with ALS</a></li><li><a href="https://www.nih.gov/news-events/nih-research-matters/learning-how-support-cells-kill-nerve-cells-als" target="_top">Learning How Support Cells Kill Nerve Cells in ALS</a></li><li><a href="https://www.nih.gov/news-events/nih-research-matters/misfolded-protein-clumps-common-dementia-lou-gehrigs-disease" target="_top">Misfolded Protein Clumps Common to Dementia, Lou Gehrig’s Disease</a></li><li><a href="https://newsinhealth.nih.gov/issue/aug2015/feature2" target="_top">All About ALS</a></li><li><a href="https://newsinhealth.nih.gov/issue/jan2014/feature1" target="_top">Dealing with Dementia</a></li></ul><p class="footnote"><strong class="label-inline">References: </strong><a href="http://www.ncbi.nlm.nih.gov/pubmed/26308891">The C9orf72 repeat expansion disrupts nucleocytoplasmic transport.</a> Zhang K, Donnelly CJ, Haeusler AR, Grima JC, Machamer JB, Steinwald P, Daley EL, Miller SJ, Cunningham KM, Vidensky S, Gupta S, Thomas MA, Hong I, Chiu SL, Huganir RL, Ostrow LW, Matunis MJ, Wang J, Sattler R, Lloyd TE, Rothstein JD. <em>Nature</em>. 2015 Sep 3;525(7567):56-61. doi: 10.1038/nature14973. Epub 2015 Aug 26. PMID: 26308891.
|
||
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||
<a href="http://www.ncbi.nlm.nih.gov/pubmed/26308899">GGGGCC repeat expansion in C9orf72 compromises nucleocytoplasmic transport.</a> Freibaum BD, Lu Y, Lopez-Gonzalez R, Kim NC, Almeida S, Lee KH, Badders N, Valentine M, Miller BL, Wong PC, Petrucelli L, Kim HJ, Gao FB, Taylor JP. <em>Nature</em>. 2015 Sep 3;525(7567):129-33. doi: 10.1038/nature14974. Epub 2015 Aug 26. PMID: 26308899.
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<a href="http://www.ncbi.nlm.nih.gov/pubmed/26308983">Modifiers of C9orf72 dipeptide repeat toxicity connect nucleocytoplasmic transport defects to FTD/ALS.</a> Jovičić A, Mertens J, Boeynaems S, Bogaert E, Chai N, Yamada SB, Paul JW 3rd, Sun S, Herdy JR, Bieri G, Kramer NJ, Gage FH, Van Den Bosch L, Robberecht W, Gitler AD. <em>Nat Neurosci</em>. 2015 Aug 26;18(9):1226-9. doi: 10.1038/nn.4085. PMID: 26308983.</p><p class="footnote"><strong class="label-inline">Funding: </strong>NIH’s National Institute of Neurological Disorders and Stroke (NINDS) and National Cancer Institute (NCI); Robert Packard Center for ALS Research at Johns Hopkins University; Muscular Dystrophy Association; Alzheimer’s Drug Discovery Foundation; Judith and Jean Pape Adams Charitable Foundation; Alzheimer’s Disease Research Center at Johns Hopkins; Maryland Technology Development Corporation (TEDCO); Target ALS Springboard Fellowship; William and Ella Owens Foundation; and ALS Association.</p>
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