α-Synuclein phosphorylation as a therapeutic target in Parkinson’s disease
Identifieur interne : 000033 ( Main/Corpus ); précédent : 000032; suivant : 000034α-Synuclein phosphorylation as a therapeutic target in Parkinson’s disease
Auteurs : Steven P. Braithwaite ; Jeffry B. Stock ; M. Maral MouradianSource :
- Reviews in the Neurosciences [ 0334-1763 ] ; 2012-04-01.
Abstract
Phosphorylation is a key post-translational modification necessary for normal cellular signaling and, therefore, lies at the heart of cellular function. In neurodegenerative disorders, abnormal hyperphosphorylation of pathogenic proteins is a common phenomenon that contributes in important ways to the disease process. A prototypical protein that is hyperphosphorylated in the brain is α-synuclein (α-syn) – found in Lewy bodies and Lewy neurites – the pathological hallmarks of Parkinson’s disease (PD) and other α-synucleinopathies. The genetic linkage of α-syn to PD as well as its pathological association in both genetic and sporadic cases have made it the primary protein of interest. In understanding how α-syn dysfunction occurs, increasing focus is being placed on its abnormal aggregation and the contribution of phosphorylation to this process. Studies of both the kinases and phosphatases that regulate α-syn phosphorylation are beginning to reveal the roles of this post-translational modification in disease pathogenesis. Modulation of α-syn phosphorylation may ultimately prove to be a viable strategy for disease-modifying therapeutic interventions. In this review, we explore mechanisms related to α-syn phosphorylation, its biophysical and functional consequences, and its role in neurodegeneration.
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DOI: 10.1515/revneuro-2011-0067
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Maral</given-names><x> </x><surname>Mouradian</surname></name><email>mouradian@umdnj.edu</email><xref ref-type="aff" rid="aff3"><sup>3</sup></xref><x>, </x></contrib><aff id="aff1"><sup>1</sup>Signum Biosciences Inc., 7 Deer Park Drive, Suite H, Monmouth Junction, NJ 08852, USA</aff><aff id="aff2"><sup>2</sup>Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA</aff><aff id="aff3"><sup>3</sup>Center for Neurodegenerative and Neuroimmunologic Diseases, Department of Neurology, UMDNJ-Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA</aff></contrib-group><author-notes><corresp>Corresponding authors</corresp></author-notes><pub-date pub-type="ppub"><day>01</day><month>04</month><year>2012</year><string-date>April 2012</string-date></pub-date><pub-date pub-type="epub"><day>21</day><month>3</month><year>2012</year></pub-date><volume>23</volume><issue>2</issue><fpage>191</fpage><lpage>198</lpage><history><date date-type="received"><day>10</day><month>11</month><year>2011</year></date><date date-type="accepted"><day>12</day><month>12</month><year>2011</year></date></history><copyright-statement>©2012 by Walter de Gruyter Berlin Boston</copyright-statement><copyright-year>2012</copyright-year><related-article related-article-type="pdf" xlink:href="revneuro-2011-0067.pdf"></related-article><abstract><title>Abstract</title><p>Phosphorylation is a key post-translational modification necessary for normal cellular signaling and, therefore, lies at the heart of cellular function. In neurodegenerative disorders, abnormal hyperphosphorylation of pathogenic proteins is a common phenomenon that contributes in important ways to the disease process. A prototypical protein that is hyperphosphorylated in the brain is α-synuclein (α-syn) – found in Lewy bodies and Lewy neurites – the pathological hallmarks of Parkinson’s disease (PD) and other α-synucleinopathies. The genetic linkage of α-syn to PD as well as its pathological association in both genetic and sporadic cases have made it the primary protein of interest. In understanding how α-syn dysfunction occurs, increasing focus is being placed on its abnormal aggregation and the contribution of phosphorylation to this process. Studies of both the kinases and phosphatases that regulate α-syn phosphorylation are beginning to reveal the roles of this post-translational modification in disease pathogenesis. Modulation of α-syn phosphorylation may ultimately prove to be a viable strategy for disease-modifying therapeutic interventions. In this review, we explore mechanisms related to α-syn phosphorylation, its biophysical and functional consequences, and its role in neurodegeneration.</p></abstract><kwd-group><title>Keywords</title><kwd>aggregation</kwd><x>, </x><kwd>casein kinase</kwd><x>, </x><kwd>GRK</kwd><x>, </x><kwd>LRRK2</kwd><x>, </x><kwd>PLK</kwd><x>, </x><kwd>PP2A</kwd></kwd-group><counts><fig-count count="1"></fig-count><table-count count="0"></table-count><ref-count count="73"></ref-count></counts></article-meta></front></article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>α-Synuclein phosphorylation as a therapeutic target in Parkinson’s disease</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>α-Synuclein phosphorylation as a therapeutic target in Parkinson’s disease</title></titleInfo><name type="personal"><namePart type="given">Steven P.</namePart><namePart type="family">Braithwaite</namePart><affiliation>Signum Biosciences Inc., 7 Deer Park Drive, Suite H, Monmouth Junction, NJ 08852, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jeffry B.</namePart><namePart type="family">Stock</namePart><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">M. Maral</namePart><namePart type="family">Mouradian</namePart><affiliation>Center for Neurodegenerative and Neuroimmunologic Diseases, Department of Neurology, UMDNJ-Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="research-article"></genre><originInfo><publisher>Walter de Gruyter</publisher><dateIssued encoding="w3cdtf">2012-04-01</dateIssued><dateCreated encoding="w3cdtf">2012-03-21</dateCreated><copyrightDate encoding="w3cdtf">2012</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType><extent unit="figures">1</extent><extent unit="references">73</extent></physicalDescription><abstract lang="en">Phosphorylation is a key post-translational modification necessary for normal cellular signaling and, therefore, lies at the heart of cellular function. In neurodegenerative disorders, abnormal hyperphosphorylation of pathogenic proteins is a common phenomenon that contributes in important ways to the disease process. A prototypical protein that is hyperphosphorylated in the brain is α-synuclein (α-syn) – found in Lewy bodies and Lewy neurites – the pathological hallmarks of Parkinson’s disease (PD) and other α-synucleinopathies. The genetic linkage of α-syn to PD as well as its pathological association in both genetic and sporadic cases have made it the primary protein of interest. In understanding how α-syn dysfunction occurs, increasing focus is being placed on its abnormal aggregation and the contribution of phosphorylation to this process. Studies of both the kinases and phosphatases that regulate α-syn phosphorylation are beginning to reveal the roles of this post-translational modification in disease pathogenesis. Modulation of α-syn phosphorylation may ultimately prove to be a viable strategy for disease-modifying therapeutic interventions. In this review, we explore mechanisms related to α-syn phosphorylation, its biophysical and functional consequences, and its role in neurodegeneration.</abstract><note type="author-notes">Corresponding authors</note><subject><genre>Keywords</genre><topic>aggregation</topic><topic>casein kinase</topic><topic>GRK</topic><topic>LRRK2</topic><topic>PLK</topic><topic>PP2A</topic></subject><relatedItem type="host"><titleInfo><title>Reviews in the Neurosciences</title></titleInfo><titleInfo type="abbreviated"><title>Reviews in the Neurosciences</title></titleInfo><genre type="Journal">journal</genre><identifier type="ISSN">0334-1763</identifier><identifier type="eISSN">2191-0200</identifier><identifier type="PublisherID">revneuro</identifier><part><date>2012</date><detail type="volume"><caption>vol.</caption><number>23</number></detail><detail type="issue"><caption>no.</caption><number>2</number></detail><extent unit="pages"><start>191</start><end>198</end></extent></part></relatedItem><relatedItem type="reviewOf"><genre>pdf</genre><identifier type="pdf">revneuro-2011-0067.pdf</identifier></relatedItem><identifier type="istex">8722F720D2FD27C8249588F01DD0D02DFFBE10B6</identifier><identifier type="DOI">10.1515/revneuro-2011-0067</identifier><identifier type="ArticleID">revneuro-2011-0067</identifier><identifier type="Related-article-Href">revneuro-2011-0067.pdf</identifier><accessCondition type="use and reproduction" contentType="copyright">©2012 by Walter de Gruyter Berlin Boston</accessCondition><recordInfo><recordContentSource>De Gruyter</recordContentSource></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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