A homologue of the Parkinson’s disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover
The Parkinson’s disease‐associated LRRK2 protein is a multidomain Roco protein with GTPase activity. Here the authors use a multidisciplinary approach to characterize the GTPase mechanism of a homologous bacterial Roco protein and give mechanistic insights into disease-causing LRRK2 mutations.
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Nature Portfolio
2017
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oai:doaj.org-article:c26addf391a34197a5007b5002985a382021-12-02T17:06:13ZA homologue of the Parkinson’s disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover10.1038/s41467-017-01103-42041-1723https://doaj.org/article/c26addf391a34197a5007b5002985a382017-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-01103-4https://doaj.org/toc/2041-1723The Parkinson’s disease‐associated LRRK2 protein is a multidomain Roco protein with GTPase activity. Here the authors use a multidisciplinary approach to characterize the GTPase mechanism of a homologous bacterial Roco protein and give mechanistic insights into disease-causing LRRK2 mutations.Egon DeyaertLina WautersGiambattista GuaitoliAlbert KonijnenbergMargaux LeemansSusanne TerheydenArsen PetrovicRodrigo GallardoLaura M. Nederveen-SchippersPanagiotis S. AthanasopoulosHenderikus PotsPeter J. M. Van HaastertFrank SobottChristian Johannes GloecknerRouslan EfremovArjan KortholtWim VerséesNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-12 (2017) |
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DOAJ |
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DOAJ |
| language |
EN |
| topic |
Science Q |
| spellingShingle |
Science Q Egon Deyaert Lina Wauters Giambattista Guaitoli Albert Konijnenberg Margaux Leemans Susanne Terheyden Arsen Petrovic Rodrigo Gallardo Laura M. Nederveen-Schippers Panagiotis S. Athanasopoulos Henderikus Pots Peter J. M. Van Haastert Frank Sobott Christian Johannes Gloeckner Rouslan Efremov Arjan Kortholt Wim Versées A homologue of the Parkinson’s disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover |
| description |
The Parkinson’s disease‐associated LRRK2 protein is a multidomain Roco protein with GTPase activity. Here the authors use a multidisciplinary approach to characterize the GTPase mechanism of a homologous bacterial Roco protein and give mechanistic insights into disease-causing LRRK2 mutations. |
| format |
article |
| author |
Egon Deyaert Lina Wauters Giambattista Guaitoli Albert Konijnenberg Margaux Leemans Susanne Terheyden Arsen Petrovic Rodrigo Gallardo Laura M. Nederveen-Schippers Panagiotis S. Athanasopoulos Henderikus Pots Peter J. M. Van Haastert Frank Sobott Christian Johannes Gloeckner Rouslan Efremov Arjan Kortholt Wim Versées |
| author_facet |
Egon Deyaert Lina Wauters Giambattista Guaitoli Albert Konijnenberg Margaux Leemans Susanne Terheyden Arsen Petrovic Rodrigo Gallardo Laura M. Nederveen-Schippers Panagiotis S. Athanasopoulos Henderikus Pots Peter J. M. Van Haastert Frank Sobott Christian Johannes Gloeckner Rouslan Efremov Arjan Kortholt Wim Versées |
| author_sort |
Egon Deyaert |
| title |
A homologue of the Parkinson’s disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover |
| title_short |
A homologue of the Parkinson’s disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover |
| title_full |
A homologue of the Parkinson’s disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover |
| title_fullStr |
A homologue of the Parkinson’s disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover |
| title_full_unstemmed |
A homologue of the Parkinson’s disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover |
| title_sort |
homologue of the parkinson’s disease-associated protein lrrk2 undergoes a monomer-dimer transition during gtp turnover |
| publisher |
Nature Portfolio |
| publishDate |
2017 |
| url |
https://doaj.org/article/c26addf391a34197a5007b5002985a38 |
| work_keys_str_mv |
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