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000139567 041__ $$aEnglish
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000139567 1001_ $$0P:(DE-HGF)0$$aDeyaert, Egon$$b0
000139567 245__ $$aA homologue of the Parkinson's disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover.
000139567 260__ $$a[London]$$bNature Publishing Group UK$$c2017
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000139567 520__ $$aMutations in LRRK2 are a common cause of genetic Parkinson's disease (PD). LRRK2 is a multi-domain Roco protein, harbouring kinase and GTPase activity. In analogy with a bacterial homologue, LRRK2 was proposed to act as a GTPase activated by dimerization (GAD), while recent reports suggest LRRK2 to exist under a monomeric and dimeric form in vivo. It is however unknown how LRRK2 oligomerization is regulated. Here, we show that oligomerization of a homologous bacterial Roco protein depends on the nucleotide load. The protein is mainly dimeric in the nucleotide-free and GDP-bound states, while it forms monomers upon GTP binding, leading to a monomer-dimer cycle during GTP hydrolysis. An analogue of a PD-associated mutation stabilizes the dimer and decreases the GTPase activity. This work thus provides insights into the conformational cycle of Roco proteins and suggests a link between oligomerization and disease-associated mutations in LRRK2.
000139567 536__ $$0G:(DE-HGF)POF3-345$$a345 - Population Studies and Genetics (POF3-345)$$cPOF3-345$$fPOF III$$x0
000139567 542__ $$2Crossref$$i2017-10-18$$uhttp://creativecommons.org/licenses/by/4.0
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000139567 650_7 $$2NLM Chemicals$$aBacterial Proteins
000139567 650_7 $$086-01-1$$2NLM Chemicals$$aGuanosine Triphosphate
000139567 650_7 $$0EC 2.7.11.1$$2NLM Chemicals$$aLeucine-Rich Repeat Serine-Threonine Protein Kinase-2
000139567 650_2 $$2MeSH$$aBacterial Proteins: chemistry
000139567 650_2 $$2MeSH$$aBacterial Proteins: genetics
000139567 650_2 $$2MeSH$$aBacterial Proteins: metabolism
000139567 650_2 $$2MeSH$$aChlorobium: chemistry
000139567 650_2 $$2MeSH$$aChlorobium: enzymology
000139567 650_2 $$2MeSH$$aChlorobium: genetics
000139567 650_2 $$2MeSH$$aDimerization
000139567 650_2 $$2MeSH$$aGuanosine Triphosphate: metabolism
000139567 650_2 $$2MeSH$$aHumans
000139567 650_2 $$2MeSH$$aHydrolysis
000139567 650_2 $$2MeSH$$aLeucine-Rich Repeat Serine-Threonine Protein Kinase-2: chemistry
000139567 650_2 $$2MeSH$$aLeucine-Rich Repeat Serine-Threonine Protein Kinase-2: genetics
000139567 650_2 $$2MeSH$$aLeucine-Rich Repeat Serine-Threonine Protein Kinase-2: metabolism
000139567 650_2 $$2MeSH$$aMutation
000139567 650_2 $$2MeSH$$aParkinson Disease: enzymology
000139567 650_2 $$2MeSH$$aParkinson Disease: genetics
000139567 650_2 $$2MeSH$$aPhosphorylation
000139567 650_2 $$2MeSH$$aProtein Structure, Tertiary
000139567 7001_ $$0P:(DE-HGF)0$$aWauters, Lina$$b1
000139567 7001_ $$0P:(DE-2719)2811633$$aGuaitoli, Giambattista$$b2$$udzne
000139567 7001_ $$0P:(DE-HGF)0$$aKonijnenberg, Albert$$b3
000139567 7001_ $$0P:(DE-HGF)0$$aLeemans, Margaux$$b4
000139567 7001_ $$0P:(DE-HGF)0$$aTerheyden, Susanne$$b5
000139567 7001_ $$0P:(DE-HGF)0$$aPetrovic, Arsen$$b6
000139567 7001_ $$0P:(DE-HGF)0$$aGallardo, Rodrigo$$b7
000139567 7001_ $$0P:(DE-HGF)0$$aNederveen-Schippers, Laura M$$b8
000139567 7001_ $$0P:(DE-HGF)0$$aAthanasopoulos, Panagiotis S$$b9
000139567 7001_ $$0P:(DE-HGF)0$$aPots, Henderikus$$b10
000139567 7001_ $$0P:(DE-HGF)0$$aVan Haastert, Peter J M$$b11
000139567 7001_ $$0P:(DE-HGF)0$$aSobott, Frank$$b12
000139567 7001_ $$0P:(DE-2719)2811291$$aGloeckner, Christian Johannes$$b13$$udzne
000139567 7001_ $$0P:(DE-HGF)0$$aEfremov, Rouslan$$b14
000139567 7001_ $$0P:(DE-HGF)0$$aKortholt, Arjan$$b15
000139567 7001_ $$0P:(DE-HGF)0$$aVersées, Wim$$b16$$eCorresponding author
000139567 77318 $$2Crossref$$3journal-article$$a10.1038/s41467-017-01103-4$$b : Springer Science and Business Media LLC, 2017-10-18$$n1$$p1008$$tNature Communications$$v8$$x2041-1723$$y2017
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