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| 001 | 139567 | ||
| 005 | 20240511120147.0 | ||
| 024 | 7 | _ | |a 10.1038/s41467-017-01103-4 |2 doi |
| 024 | 7 | _ | |a pmid:29044096 |2 pmid |
| 024 | 7 | _ | |a pmc:PMC5714945 |2 pmc |
| 024 | 7 | _ | |a altmetric:27591533 |2 altmetric |
| 037 | _ | _ | |a DZNE-2020-05889 |
| 041 | _ | _ | |a English |
| 082 | _ | _ | |a 500 |
| 100 | 1 | _ | |a Deyaert, Egon |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a A homologue of the Parkinson's disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover. |
| 260 | _ | _ | |a [London] |c 2017 |b Nature Publishing Group UK |
| 264 | _ | 1 | |3 online |2 Crossref |b Springer Science and Business Media LLC |c 2017-10-18 |
| 264 | _ | 1 | |3 print |2 Crossref |b Springer Science and Business Media LLC |c 2017-12-01 |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1715348604_4833 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a Mutations in LRRK2 are a common cause of genetic Parkinson's disease (PD). LRRK2 is a multi-domain Roco protein, harbouring kinase and GTPase activity. In analogy with a bacterial homologue, LRRK2 was proposed to act as a GTPase activated by dimerization (GAD), while recent reports suggest LRRK2 to exist under a monomeric and dimeric form in vivo. It is however unknown how LRRK2 oligomerization is regulated. Here, we show that oligomerization of a homologous bacterial Roco protein depends on the nucleotide load. The protein is mainly dimeric in the nucleotide-free and GDP-bound states, while it forms monomers upon GTP binding, leading to a monomer-dimer cycle during GTP hydrolysis. An analogue of a PD-associated mutation stabilizes the dimer and decreases the GTPase activity. This work thus provides insights into the conformational cycle of Roco proteins and suggests a link between oligomerization and disease-associated mutations in LRRK2. |
| 536 | _ | _ | |a 345 - Population Studies and Genetics (POF3-345) |0 G:(DE-HGF)POF3-345 |c POF3-345 |f POF III |x 0 |
| 542 | _ | _ | |i 2017-10-18 |2 Crossref |u http://creativecommons.org/licenses/by/4.0 |
| 588 | _ | _ | |a Dataset connected to CrossRef, PubMed, |
| 650 | _ | 7 | |a Bacterial Proteins |2 NLM Chemicals |
| 650 | _ | 7 | |a Guanosine Triphosphate |0 86-01-1 |2 NLM Chemicals |
| 650 | _ | 7 | |a Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 |0 EC 2.7.11.1 |2 NLM Chemicals |
| 650 | _ | 2 | |a Bacterial Proteins: chemistry |2 MeSH |
| 650 | _ | 2 | |a Bacterial Proteins: genetics |2 MeSH |
| 650 | _ | 2 | |a Bacterial Proteins: metabolism |2 MeSH |
| 650 | _ | 2 | |a Chlorobium: chemistry |2 MeSH |
| 650 | _ | 2 | |a Chlorobium: enzymology |2 MeSH |
| 650 | _ | 2 | |a Chlorobium: genetics |2 MeSH |
| 650 | _ | 2 | |a Dimerization |2 MeSH |
| 650 | _ | 2 | |a Guanosine Triphosphate: metabolism |2 MeSH |
| 650 | _ | 2 | |a Humans |2 MeSH |
| 650 | _ | 2 | |a Hydrolysis |2 MeSH |
| 650 | _ | 2 | |a Leucine-Rich Repeat Serine-Threonine Protein Kinase-2: chemistry |2 MeSH |
| 650 | _ | 2 | |a Leucine-Rich Repeat Serine-Threonine Protein Kinase-2: genetics |2 MeSH |
| 650 | _ | 2 | |a Leucine-Rich Repeat Serine-Threonine Protein Kinase-2: metabolism |2 MeSH |
| 650 | _ | 2 | |a Mutation |2 MeSH |
| 650 | _ | 2 | |a Parkinson Disease: enzymology |2 MeSH |
| 650 | _ | 2 | |a Parkinson Disease: genetics |2 MeSH |
| 650 | _ | 2 | |a Phosphorylation |2 MeSH |
| 650 | _ | 2 | |a Protein Structure, Tertiary |2 MeSH |
| 700 | 1 | _ | |a Wauters, Lina |0 P:(DE-HGF)0 |b 1 |
| 700 | 1 | _ | |a Guaitoli, Giambattista |0 P:(DE-2719)2811633 |b 2 |u dzne |
| 700 | 1 | _ | |a Konijnenberg, Albert |0 P:(DE-HGF)0 |b 3 |
| 700 | 1 | _ | |a Leemans, Margaux |0 P:(DE-HGF)0 |b 4 |
| 700 | 1 | _ | |a Terheyden, Susanne |0 P:(DE-HGF)0 |b 5 |
| 700 | 1 | _ | |a Petrovic, Arsen |0 P:(DE-HGF)0 |b 6 |
| 700 | 1 | _ | |a Gallardo, Rodrigo |0 P:(DE-HGF)0 |b 7 |
| 700 | 1 | _ | |a Nederveen-Schippers, Laura M |0 P:(DE-HGF)0 |b 8 |
| 700 | 1 | _ | |a Athanasopoulos, Panagiotis S |0 P:(DE-HGF)0 |b 9 |
| 700 | 1 | _ | |a Pots, Henderikus |0 P:(DE-HGF)0 |b 10 |
| 700 | 1 | _ | |a Van Haastert, Peter J M |0 P:(DE-HGF)0 |b 11 |
| 700 | 1 | _ | |a Sobott, Frank |0 P:(DE-HGF)0 |b 12 |
| 700 | 1 | _ | |a Gloeckner, Christian Johannes |0 P:(DE-2719)2811291 |b 13 |u dzne |
| 700 | 1 | _ | |a Efremov, Rouslan |0 P:(DE-HGF)0 |b 14 |
| 700 | 1 | _ | |a Kortholt, Arjan |0 P:(DE-HGF)0 |b 15 |
| 700 | 1 | _ | |a Versées, Wim |0 P:(DE-HGF)0 |b 16 |e Corresponding author |
| 773 | 1 | 8 | |a 10.1038/s41467-017-01103-4 |b : Springer Science and Business Media LLC, 2017-10-18 |n 1 |p 1008 |3 journal-article |2 Crossref |t Nature Communications |v 8 |y 2017 |x 2041-1723 |
| 773 | _ | _ | |a 10.1038/s41467-017-01103-4 |g Vol. 8, no. 1, p. 1008 |0 PERI:(DE-600)2553671-0 |n 1 |q 8:1<1008 |p 1008 |t Nature Communications |v 8 |y 2017 |x 2041-1723 |
| 856 | 4 | _ | |y OpenAccess |u https://pub.dzne.de/record/139567/files/DZNE-2020-05889.pdf |
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| 856 | 7 | _ | |2 Pubmed Central |u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5714945 |
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