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000140566 1001_ $$0P:(DE-2719)9000090$$aFunk, Natalja$$b0$$eFirst author$$udzne
000140566 245__ $$aThe Parkinson's disease-linked Leucine-rich repeat kinase 2 (LRRK2) is required for insulin-stimulated translocation of GLUT4.
000140566 260__ $$a[London]$$bMacmillan Publishers Limited, part of Springer Nature$$c2019
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000140566 520__ $$aMutations within Leucine-rich repeat kinase 2 (LRRK2) are associated with late-onset Parkinson's disease. The physiological function of LRRK2 and molecular mechanism underlying the pathogenic role of LRRK2 mutations remain uncertain. Here, we investigated the role of LRRK2 in intracellular signal transduction. We find that deficiency of Lrrk2 in rodents affects insulin-dependent translocation of glucose transporter type 4 (GLUT4). This deficit is restored during aging by prolonged insulin-dependent activation of protein kinase B (PKB, Akt) and Akt substrate of 160 kDa (AS160), and is compensated by elevated basal expression of GLUT4 on the cell surface. Furthermore, we find a crucial role of Rab10 phosphorylation by LRRK2 for efficient insulin signal transduction. Translating our findings into human cell lines, we find comparable molecular alterations in fibroblasts from Parkinson's patients with the known pathogenic G2019S LRRK2 mutation. Our results highlight the role of LRRK2 in insulin-dependent signalling with potential therapeutic implications.
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000140566 536__ $$0G:(DE-HGF)POF3-342$$a342 - Disease Mechanisms and Model Systems (POF3-342)$$cPOF3-342$$fPOF III$$x1
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000140566 650_2 $$2MeSH$$aAnimals
000140566 650_2 $$2MeSH$$aCell Survival: drug effects
000140566 650_2 $$2MeSH$$aFibroblast Growth Factors: pharmacology
000140566 650_2 $$2MeSH$$aFibroblasts: cytology
000140566 650_2 $$2MeSH$$aFibroblasts: metabolism
000140566 650_2 $$2MeSH$$aGlucose Transporter Type 4: metabolism
000140566 650_2 $$2MeSH$$aHumans
000140566 650_2 $$2MeSH$$aInsulin: pharmacology
000140566 650_2 $$2MeSH$$aLeucine-Rich Repeat Serine-Threonine Protein Kinase-2: genetics
000140566 650_2 $$2MeSH$$aLeucine-Rich Repeat Serine-Threonine Protein Kinase-2: metabolism
000140566 650_2 $$2MeSH$$aMice
000140566 650_2 $$2MeSH$$aNeuronal Outgrowth: drug effects
000140566 650_2 $$2MeSH$$aParkinson Disease: metabolism
000140566 650_2 $$2MeSH$$aParkinson Disease: pathology
000140566 650_2 $$2MeSH$$aPhosphorylation
000140566 650_2 $$2MeSH$$aPolymorphism, Single Nucleotide
000140566 650_2 $$2MeSH$$aProto-Oncogene Proteins c-akt: metabolism
000140566 650_2 $$2MeSH$$aRats
000140566 650_2 $$2MeSH$$aSignal Transduction: drug effects
000140566 650_2 $$2MeSH$$arab GTP-Binding Proteins: metabolism
000140566 7001_ $$0P:(DE-2719)9000226$$aMunz, Marita$$b1$$udzne
000140566 7001_ $$0P:(DE-HGF)0$$aOtt, Thomas$$b2
000140566 7001_ $$0P:(DE-2719)2811916$$aBrockmann, Kathrin$$b3$$udzne
000140566 7001_ $$0P:(DE-2719)2810261$$aWenninger-Weinzierl, Andrea$$b4$$udzne
000140566 7001_ $$0P:(DE-HGF)0$$aKühn, Ralf$$b5
000140566 7001_ $$0P:(DE-HGF)0$$aVogt-Weisenhorn, Daniela$$b6
000140566 7001_ $$0P:(DE-HGF)0$$aGiesert, Florian$$b7
000140566 7001_ $$0P:(DE-2719)2000028$$aWurst, Wolfgang$$b8$$udzne
000140566 7001_ $$0P:(DE-2719)2320009$$aGasser, Thomas$$b9$$udzne
000140566 7001_ $$0P:(DE-2719)9000027$$aBiskup, Saskia$$b10$$eLast author$$udzne
000140566 77318 $$2Crossref$$3journal-article$$a10.1038/s41598-019-40808-y$$b : Springer Science and Business Media LLC, 2019-03-14$$n1$$p4515$$tScientific Reports$$v9$$x2045-2322$$y2019
000140566 773__ $$0PERI:(DE-600)2615211-3$$a10.1038/s41598-019-40808-y$$gVol. 9, no. 1, p. 4515$$n1$$p4515$$q9:1<4515$$tScientific reports$$v9$$x2045-2322$$y2019
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