Phosphatases of α-synuclein, LRRK2, and tau: important players in the phosphorylation-dependent pathology of Parkinsonism
Identifieur interne : 000930 ( Pmc/Curation ); précédent : 000929; suivant : 000931Phosphatases of α-synuclein, LRRK2, and tau: important players in the phosphorylation-dependent pathology of Parkinsonism
Auteurs : Jean-Marc Taymans ; Veerle BaekelandtSource :
- Frontiers in Genetics [ 1664-8021 ] ; 2014.
Abstract
An important challenge in the field of Parkinson’s disease (PD) is to develop disease modifying therapies capable of stalling or even halting disease progression. Coupled to this challenge is the need to identify disease biomarkers, in order to identify pre-symptomatic hallmarks of disease and monitor disease progression. The answer to these challenges lies in the elucidation of the molecular causes underlying PD, for which important leads are disease genes identified in studies investigating the underlying genetic causes of PD. LRRK2 and α-syn have been both linked to familial forms of PD as well as associated to sporadic PD. Another gene, microtubule associated protein tau (MAPT), has been genetically linked to a dominant form of frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17) and genome-wide association studies report a strong association between MAPT and sporadic PD. Interestingly, LRRK2, α-syn, and tau are all phosphorylated proteins, and their phosphorylation patterns are linked to disease. In this review, we provide an overview of the evidence linking LRRK2, α-syn, and tau phosphorylation to PD pathology and focus on studies which have identified phosphatases responsible for dephosphorylation of pathology-related phosphorylations. We also discuss how the LRRK2, α-syn, and tau phosphatases may point to separate or cross-talking pathological pathways in PD. Finally, we will discuss how the study of phosphatases of dominant Parkinsonism proteins opens perspectives for targeting pathological phosphorylation events.
Url:
DOI: 10.3389/fgene.2014.00382
PubMed: 25426138
PubMed Central: 4224088
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Phosphatases of α-synuclein, LRRK2, and tau: important players in the phosphorylation-dependent pathology of Parkinsonism</title><author><name sortKey="Taymans, Jean Marc" sort="Taymans, Jean Marc" uniqKey="Taymans J" first="Jean-Marc" last="Taymans">Jean-Marc Taymans</name></author><author><name sortKey="Baekelandt, Veerle" sort="Baekelandt, Veerle" uniqKey="Baekelandt V" first="Veerle" last="Baekelandt">Veerle Baekelandt</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">25426138</idno><idno type="pmc">4224088</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4224088</idno><idno type="RBID">PMC:4224088</idno><idno type="doi">10.3389/fgene.2014.00382</idno><date when="2014">2014</date><idno type="wicri:Area/Pmc/Corpus">000934</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000934</idno><idno type="wicri:Area/Pmc/Curation">000930</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000930</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Phosphatases of α-synuclein, LRRK2, and tau: important players in the phosphorylation-dependent pathology of Parkinsonism</title><author><name sortKey="Taymans, Jean Marc" sort="Taymans, Jean Marc" uniqKey="Taymans J" first="Jean-Marc" last="Taymans">Jean-Marc Taymans</name></author><author><name sortKey="Baekelandt, Veerle" sort="Baekelandt, Veerle" uniqKey="Baekelandt V" first="Veerle" last="Baekelandt">Veerle Baekelandt</name></author></analytic><series><title level="j">Frontiers in Genetics</title><idno type="eISSN">1664-8021</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>An important challenge in the field of Parkinson’s disease (PD) is to develop disease modifying therapies capable of stalling or even halting disease progression. Coupled to this challenge is the need to identify disease biomarkers, in order to identify pre-symptomatic hallmarks of disease and monitor disease progression. The answer to these challenges lies in the elucidation of the molecular causes underlying PD, for which important leads are disease genes identified in studies investigating the underlying genetic causes of PD. LRRK2 and α-syn have been both linked to familial forms of PD as well as associated to sporadic PD. Another gene, microtubule associated protein tau (MAPT), has been genetically linked to a dominant form of frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17) and genome-wide association studies report a strong association between MAPT and sporadic PD. Interestingly, LRRK2, α-syn, and tau are all phosphorylated proteins, and their phosphorylation patterns are linked to disease. In this review, we provide an overview of the evidence linking LRRK2, α-syn, and tau phosphorylation to PD pathology and focus on studies which have identified phosphatases responsible for dephosphorylation of pathology-related phosphorylations. We also discuss how the LRRK2, α-syn, and tau phosphatases may point to separate or cross-talking pathological pathways in PD. Finally, we will discuss how the study of phosphatases of dominant Parkinsonism proteins opens perspectives for targeting pathological phosphorylation events.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Anderson, J P" uniqKey="Anderson J">J. P. Anderson</name></author><author><name sortKey="Walker, D E" uniqKey="Walker D">D. E. Walker</name></author><author><name sortKey="Goldstein, J M" uniqKey="Goldstein J">J. M. Goldstein</name></author><author><name sortKey="De Laat, R" uniqKey="De Laat R">R. 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Front Genet</journal-id><journal-id journal-id-type="iso-abbrev">Front Genet</journal-id><journal-id journal-id-type="publisher-id">Front. Genet.</journal-id><journal-title-group><journal-title>Frontiers in Genetics</journal-title></journal-title-group><issn pub-type="epub">1664-8021</issn><publisher><publisher-name>Frontiers Media S.A.</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">25426138</article-id><article-id pub-id-type="pmc">4224088</article-id><article-id pub-id-type="doi">10.3389/fgene.2014.00382</article-id><article-categories><subj-group subj-group-type="heading"><subject>Genetics</subject><subj-group><subject>Review Article</subject></subj-group></subj-group></article-categories><title-group><article-title>Phosphatases of α-synuclein, LRRK2, and tau: important players in the phosphorylation-dependent pathology of Parkinsonism</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Taymans</surname><given-names>Jean-Marc</given-names></name><xref ref-type="author-notes" rid="fn002"><sup>*</sup></xref><uri xlink:type="simple" xlink:href="http://community.frontiersin.org/people/u/112549"></uri></contrib><contrib contrib-type="author"><name><surname>Baekelandt</surname><given-names>Veerle</given-names></name><uri xlink:type="simple" xlink:href="http://community.frontiersin.org/people/u/91372"></uri></contrib></contrib-group><aff id="aff1"><institution>Department of Neurosciences, Laboratory for Neurobiology and Gene Therapy, KU Leuven</institution><country>Leuven, Belgium</country></aff><author-notes><fn fn-type="edited-by"><p>Edited by: <italic>Allegra Via, Sapienza University, Italy; Andreas Zanzoni, Inserm Technological Advances for Genomics and Clinics, UMR1090, France</italic></p></fn><fn fn-type="edited-by"><p>Reviewed by: <italic>Eric Yang, Johnson and Johnson, USA; Christian Johannes Gloeckner, Helmholtz Zentrum München, Germany</italic></p></fn><corresp id="fn002">*Correspondence: <italic>Jean-Marc Taymans, Jean-Pierre Aubert Research Center, UMR837, Rue Polonovski – 1 Place de Verdun, 59045 Lille, France e-mail: <email xlink:type="simple">jean-marc.taymans@inserm.fr</email></italic></corresp><fn fn-type="other" id="fn001"><p>This article was submitted to Systems Biology, a section of the journal Frontiers in Genetics.</p></fn></author-notes><pub-date pub-type="epub"><day>07</day><month>11</month><year>2014</year></pub-date><pub-date pub-type="collection"><year>2014</year></pub-date><volume>5</volume><elocation-id>382</elocation-id><history><date date-type="received"><day>21</day><month>6</month><year>2014</year></date><date date-type="accepted"><day>17</day><month>10</month><year>2014</year></date></history><permissions><copyright-statement>Copyright © 2014 Taymans and Baekelandt.</copyright-statement><copyright-year>2014</copyright-year><license license-type="open-access" xlink:href="http://creativecommons.org/licenses/by/4.0/"><license-p> This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.</license-p></license></permissions><abstract><p>An important challenge in the field of Parkinson’s disease (PD) is to develop disease modifying therapies capable of stalling or even halting disease progression. Coupled to this challenge is the need to identify disease biomarkers, in order to identify pre-symptomatic hallmarks of disease and monitor disease progression. The answer to these challenges lies in the elucidation of the molecular causes underlying PD, for which important leads are disease genes identified in studies investigating the underlying genetic causes of PD. LRRK2 and α-syn have been both linked to familial forms of PD as well as associated to sporadic PD. Another gene, microtubule associated protein tau (MAPT), has been genetically linked to a dominant form of frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17) and genome-wide association studies report a strong association between MAPT and sporadic PD. Interestingly, LRRK2, α-syn, and tau are all phosphorylated proteins, and their phosphorylation patterns are linked to disease. In this review, we provide an overview of the evidence linking LRRK2, α-syn, and tau phosphorylation to PD pathology and focus on studies which have identified phosphatases responsible for dephosphorylation of pathology-related phosphorylations. We also discuss how the LRRK2, α-syn, and tau phosphatases may point to separate or cross-talking pathological pathways in PD. Finally, we will discuss how the study of phosphatases of dominant Parkinsonism proteins opens perspectives for targeting pathological phosphorylation events.</p></abstract><kwd-group><kwd>PP1</kwd><kwd>PP2A</kwd><kwd>phosphorylation</kwd><kwd>phosphatase</kwd><kwd>Parkinson disease</kwd><kwd>LRRK2</kwd><kwd>alpha-synuclein</kwd><kwd>tauopathies</kwd><kwd>tau proteins</kwd></kwd-group><counts><fig-count count="4"></fig-count><table-count count="3"></table-count><equation-count count="0"></equation-count><ref-count count="106"></ref-count><page-count count="12"></page-count><word-count count="0"></word-count></counts></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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