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Systematic proteomic analysis of LRRK2-mediated Rab GTPase phosphorylation establishes a connection to ciliogenesis
Abstract
We previously reported that Parkinson’s disease (PD) kinase LRRK2 phosphorylates a subset of Rab GTPases on a conserved residue in their switch-II domains (Steger et al., 2016) (PMID: 26824392). Here, we systematically analyzed the Rab protein family and found 14 of them (Rab3A/B/C/D, Rab5A/B/C, Rab8A/B, Rab10, Rab12, Rab29, Rab35 and Rab43) to be specifically phosphorylated by LRRK2, with evidence for endogenous phosphorylation for ten of them (Rab3A/B/C/D, Rab8A/B, Rab10, Rab12, Rab35 and Rab43). Affinity enrichment mass spectrometry revealed that the primary ciliogenesis regulator, RILPL1 specifically interacts with the LRRK2-phosphorylated forms of Rab8A and Rab10, whereas RILPL2 binds to phosphorylated Rab8A, Rab10, and Rab12. Induction of primary cilia formation by serum starvation led to a two-fold reduction in ciliogenesis in fibroblasts derived from pathogenic LRRK2-R1441G knock-in mice. These results implicate LRRK2 in primary ciliogenesis and suggest that Rab-mediated protein transport and/or signaling defects at cilia may contribute to LRRK2-dependent pathologies.
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LRRK2 phosphorylates Rab10 at threonine 73 (pT73Rab10).
“Rab10 in particular has been validated in multiple studies as a substrate for LRRK2 which phosphorylates threonine 73 (pT73Rab10) in the switch II domain involved in effector binding [78, 79].”
From Cellular and subcellular localization of Rab10 and phospho-T73 Rab10 in the mouse and human brain (2023) · cites this paper as [78]
The G2019S-LRRK2 mutation increases LRRK2 kinase activity.
“The most common mutation, G2019S-LRRK2, increases the kinase activity of LRRK2 causing hyper-phosphorylation of its substrates.”
From Cellular and subcellular localization of Rab10 and phospho-T73 Rab10 in the mouse and human brain (2023) · cites this paper as [78]
Recent phosphoproteomic analyses identified RAB3, RAB8, RAB10, RAB12, RAB35, and RAB43 as endogenous substrates for LRRK2 activity.
“Recent phosphoproteomic analyses identified a small subset of RAB GTPases (RAB3, RAB8, RAB10, RAB12, RAB35, and RAB43) as endogenous substrates for the LRRK2 activity [12].”
From Distinct Roles for RAB10 and RAB29 in Pathogenic LRRK2-Mediated Endolysosomal Trafficking Alterations (2020) · cites this paper as [12]
Cargo adaptor proteins from the RILP family (RILPL1 and RILPL2) involved in ciliogenesis bind tightly with some phosphorylated Rabs including Rab10, but not with unphosphorylated Rabs.
“For example, cargo adaptor proteins from the RILP (Rab interacting lysosomal protein like) family (RILPL1 and RILPL2) involved in ciliogenesis, bind tightly with some of the phosphorylated Rabs including Rab10, but not with the unphosphorylated Rabs [35, 78].”
From Cellular and subcellular localization of Rab10 and phospho-T73 Rab10 in the mouse and human brain (2023) · cites this paper as [78]
Phosphorylation not only interferes with the interaction of Rabs with its effector proteins, but in a few cases facilitates alternative interactions of Rabs with a completely new effector protein when they are phosphorylated.
“Studies show that phosphorylation not only interferes with the interaction of Rabs with its effector proteins, but in a few cases facilitates alternative interactions of Rabs with a completely new effector protein when they are phosphorylated [78].”
From Cellular and subcellular localization of Rab10 and phospho-T73 Rab10 in the mouse and human brain (2023) · cites this paper as [78]
RAB7A does not serve as a substrate for the LRRK2 kinase activity in vitro or in intact cells.
“RAB7A does not serve as a substrate for the LRRK2 kinase activity in vitro or in intact cells [12,18,31]”
From Distinct Roles for RAB10 and RAB29 in Pathogenic LRRK2-Mediated Endolysosomal Trafficking Alterations (2020) · cites this paper as [12]
RAB10 serves as a prominent LRRK2 kinase substrate in all cell lines and tissues analyzed.
“RAB10 serves as a prominent LRRK2 kinase substrate in all cell lines and tissues analyzed [12,18,32,33,34,35].”
From Distinct Roles for RAB10 and RAB29 in Pathogenic LRRK2-Mediated Endolysosomal Trafficking Alterations (2020) · cites this paper as [12]
LRRK2 phosphorylates RAB proteins on their switch II regions, interfering with their binding to most regulatory and effector proteins.
“LRRK2 phosphorylates the RAB proteins on their switch II regions, which consequently interferes with their binding to most regulatory and effector proteins [12,18,19].”
From Distinct Roles for RAB10 and RAB29 in Pathogenic LRRK2-Mediated Endolysosomal Trafficking Alterations (2020) · cites this paper as [12]
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Citations
Cites
International Parkinson's Disease Genomics Consortium (IPDGC), Nalls, M. A., Parkinson's Study Group (PSG) Parkinson's Research: The Organized GENetics Initiative (PROGENI), 23andMe, GenePD, NeuroGenetics Research Consortium (NGRC), Hussman Institute of Human Genomics (HIHG), Investigator, T. A. J. D., (CHARGE), C. F. H. A. A. R. I. G. E., North American Brain Expression Consortium (NABEC), et al. (2014) · Nature Genetics · doi:10.1038/ng.3043 · Cited by 1,895
Kulak, N. A., Pichler, G., Paron, I., Nagaraj, N., & Mann, M. (2014) · Nature Methods · doi:10.1038/nmeth.2834 · Cited by 1,719
Self-citationGenes and molecular pathways underpinning ciliopathies
Reiter, J. F., & Leroux, M. R. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.60 · Cited by 1,588
Nachury, M. V., Loktev, A. V., Zhang, Q., Westlake, C. J., Peränen, J., Merdes, A., Slusarski, D. C., Scheller, R. H., Bazan, J. F., Sheffield, V. C., et al. (2007) · Cell · doi:10.1016/j.cell.2007.03.053 · Cited by 1,384
Rab Proteins and the Compartmentalization of the Endosomal System
Wandinger-Ness, A., & Zerial, M. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022616 · Cited by 586
Jenkins, D., Seelow, D., Jehee, F. S., Perlyn, C. A., Alonso, L. G., Bueno, D. F., Donnai, D., Josifiova, D., Mathijssen, I. M. J., Morton, J. E. V., et al. (2007) · The American Journal of Human Genetics · doi:10.1086/518047 · Cited by 276
Systems‐wide analysis of BCR signalosomes and downstream phosphorylation and ubiquitylation
Satpathy, S., Wagner, S. A., Beli, P., Gupta, R., Kristiansen, T. A., Malinova, D., Francavilla, C., Tolar, P., Bishop, G. A., Hostager, B. S., et al. (2015) · Molecular Systems Biology · doi:10.15252/msb.20145880 · Cited by 124
Matsui, T., Ohbayashi, N., & Fukuda, M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.370544 · Cited by 90
Flagged first, then by citations
Research works printed but not linked: 54
- Baptista, 2013, Loss of leucine-rich repeat kinase 2 (LRRK2) in rats leads to progressive abnormal phenotypes in peripheral organs, PLoS ONE, 8, e80705, 10.1371/journal.pone.0080705 · DOI
- Bardien, 2011, Genetic characteristics of leucine-rich repeat kinase 2 (LRRK2) associated Parkinson's disease, Parkinsonism & Related Disorders, 17, 501, 10.1016/j.parkreldis.2010.11.008 · DOI
- Beilina, 2016, Genes associated with Parkinson's disease: regulation of autophagy and beyond, Journal of Neurochemistry, 139, 91, 10.1111/jnc.13266 · DOI
- Beilina, 2014, Unbiased screen for interactors of leucine-rich repeat kinase 2 supports a common pathway for sporadic and familial Parkinson disease, PNAS, 111, 2626, 10.1073/pnas.1318306111 · DOI · Paper page
- Boehlke, 2010, Differential role of Rab proteins in ciliary trafficking: Rab23 regulates smoothened levels, Journal of Cell Science, 123, 1460, 10.1242/jcs.058883 · DOI · Paper page
- Choi, 2012, Brain penetrant LRRK2 inhibitor, ACS Medicinal Chemistry Letters, 3, 658, 10.1021/ml300123a · DOI
- Cookson, 2010, The role of leucine-rich repeat kinase 2 (LRRK2) in Parkinson's disease, Nature Reviews Neuroscience, 11, 791, 10.1038/nrn2935 · DOI
- Cookson, 2016, Cellular functions of LRRK2 implicate vesicular trafficking pathways in Parkinson's disease, Biochemical Society Transactions, 44, 1603, 10.1042/BST20160228 · DOI
- Cox, 2014, Accurate proteome-wide label-free quantification by delayed normalization and maximal peptide ratio extraction, termed MaxLFQ, Molecular & Cellular Proteomics, 13, 2513, 10.1074/mcp.M113.031591 · DOI · Paper page
- Cox, 2008, MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification, Nature Biotechnology, 26, 1367, 10.1038/nbt.1511 · DOI · Paper page
- Cox, 2011, Andromeda: a peptide search engine integrated into the MaxQuant environment, Journal of Proteome Research, 10, 1794, 10.1021/pr101065j · DOI
- Dzamko, 2012, The IkappaB kinase family phosphorylates the Parkinson's disease kinase LRRK2 at Ser935 and Ser910 during toll-like receptor signaling, PLoS One, 7, e39132, 10.1371/journal.pone.0039132 · DOI
- Fell, 2015, MLi-2, a potent, selective, and centrally active compound for exploring the therapeutic potential and safety of LRRK2 kinase inhibition, Journal of Pharmacology and Experimental Therapeutics, 355, 397, 10.1124/jpet.115.227587 · DOI
- Funayama, 2005, An LRRK2 mutation as a cause for the parkinsonism in the original PARK8 family, Annals of Neurology, 57, 918, 10.1002/ana.20484 · DOI
- Gerber, 2003, Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS, PNAS, 100, 6940, 10.1073/pnas.0832254100 · DOI · Paper page
- Giaime, 2017, Age-dependent dopaminergic neurodegeneration and impairment of the autophagy-lysosomal pathway in lrrk-deficient mice, Neuron, 10.1016/j.neuron.2017.09.036 · DOI
- Giesert, 2013, Expression analysis of Lrrk1, Lrrk2 and Lrrk2 splice variants in mice, PLoS ONE, 8, e63778, 10.1371/journal.pone.0063778 · DOI
- Goody, 2012, Reversible phosphocholination of Rab proteins by Legionella pneumophila effector proteins, The EMBO Journal, 31, 1774, 10.1038/emboj.2012.16 · DOI
- Hou, 2011, A structural basis for Lowe syndrome caused by mutations in the Rab-binding domain of OCRL1, The EMBO Journal, 30, 1659, 10.1038/emboj.2011.60 · DOI
- Ito, 2016, Phos-tag analysis of Rab10 phosphorylation by LRRK2: a powerful assay for assessing kinase function and inhibitors, Biochemical Journal, 473, 2671, 10.1042/BCJ20160557 · DOI · Paper page
- Jensen, 2016, Whole-organism developmental expression profiling identifies rab-28 as a novel ciliary gtpase associated with the bbsome and intraflagellar transport, PLOS Genetics, 12, e1006469, 10.1371/journal.pgen.1006469 · DOI
- Jordens, 2001, The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors, Current Biology, 11, 1680, 10.1016/S0960-9822(01)00531-0 · DOI · Paper page
- Knödler, 2010, Coordination of Rab8 and Rab11 in primary ciliogenesis, PNAS, 107, 6346, 10.1073/pnas.1002401107 · DOI
- Kuwahara, 2016, LRRK2 and RAB7L1 coordinately regulate axonal morphology and lysosome integrity in diverse cellular contexts, Scientific Reports, 6, 29945, 10.1038/srep29945 · DOI · Paper page
- Levin, 2016, Innate immunity kinase TAK1 phosphorylates Rab1 on a hotspot for posttranslational modifications by host and pathogen, PNAS, 113, E4776, 10.1073/pnas.1608355113 · DOI
- Lis, 2017, Development of phospho-specific Rab protein antibodies to monitor in vivo activity of the LRRK2 Parkinson's disease kinase, Biochemical Journal, BCJ20170802, 10.1042/BCJ20170802 · DOI · Paper page
- Liu, 2016, Negative regulation of phosphatidylinositol 3-phosphate levels in early-to-late endosome conversion, The Journal of Cell Biology, 212, 181, 10.1083/jcb.201506081 · DOI
- MacLean, 2010, Skyline: an open source document editor for creating and analyzing targeted proteomics experiments, Bioinformatics, 26, 966, 10.1093/bioinformatics/btq054 · DOI · Paper page
- Malicki, 2017, The Cilium: Cellular Antenna and Central Processing Unit, Trends in Cell Biology, 27, 126, 10.1016/j.tcb.2016.08.002 · DOI
- Mukherjee, 2011, Modulation of Rab GTPase function by a protein phosphocholine transferase, Nature, 477, 103, 10.1038/nature10335 · DOI
- Müller, 2010, The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b, Science, 329, 946, 10.1126/science.1192276 · DOI
- Nichols, 2010, 14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization, Biochemical Journal, 430, 393, 10.1042/BJ20100483 · DOI
- Oesterlin, 2012, Posttranslational modifications of Rab proteins cause effective displacement of GDP dissociation inhibitor, PNAS, 109, 5621, 10.1073/pnas.1121161109 · DOI
- Onnis, 2015, The small GTPase Rab29 is a common regulator of immune synapse assembly and ciliogenesis, Cell Death and Differentiation, 22, 1687, 10.1038/cdd.2015.17 · DOI · Paper page
- Paisán-Ruíz, 2004, Cloning of the gene containing mutations that cause PARK8-linked Parkinson's disease, Neuron, 44, 595, 10.1016/j.neuron.2004.10.023 · DOI
- Rappsilber, 2003, Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics, Analytical Chemistry, 75, 663, 10.1021/ac026117i · DOI
- Roosing, 2013, Mutations in RAB28, encoding a farnesylated small GTPase, are associated with autosomal-recessive cone-rod dystrophy, The American Journal of Human Genetics, 93, 110, 10.1016/j.ajhg.2013.05.005 · DOI
- Sato, 2014, Rab8a and Rab8b are essential for several apical transport pathways but insufficient for ciliogenesis, Journal of Cell Science, 127, 422, 10.1242/jcs.136903 · DOI
- Schapansky, 2014, Membrane recruitment of endogenous LRRK2 precedes its potent regulation of autophagy, Human Molecular Genetics, 23, 4201, 10.1093/hmg/ddu138 · DOI · Paper page
- Schaub, 2013, The Rilp-like proteins Rilpl1 and Rilpl2 regulate ciliary membrane content, Molecular Biology of the Cell, 24, 453, 10.1091/mbc.E12-08-0598 · DOI
- Sheng, 2012, Ser1292 autophosphorylation is an indicator of lrrk2 kinase activity and contributes to the cellular effects of pd mutations, Science Translational Medicine, 4, 3004485, 10.1126/scitranslmed.3004485 · DOI
- Simón-Sánchez, 2009, Genome-wide association study reveals genetic risk underlying Parkinson's disease, Nature Genetics, 41, 1308, 10.1038/ng.487 · DOI · Paper page
- Steger, 2016, Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates a subset of Rab GTPases, eLife, 5, e12813, 10.7554/eLife.12813 · DOI · Paper page
- Tang, 2017, Rabs, membrane dynamics, and parkinson's disease, Journal of Cellular Physiology, 232, 1626, 10.1002/jcp.25713 · DOI
- Thirstrup, 2017, Selective LRRK2 kinase inhibition reduces phosphorylation of endogenous Rab10 and Rab12 in human peripheral mononuclear blood cells, Scientific Reports, 7, 10300, 10.1038/s41598-017-10501-z · DOI
- Thévenet, 2011, Regulation of LRRK2 expression points to a functional role in human monocyte maturation, PLoS One, 6, e21519, 10.1371/journal.pone.0021519 · DOI
- Tyanova, 2016, The Perseus computational platform for comprehensive analysis of (prote)omics data, Nature Methods, 13, 731, 10.1038/nmeth.3901 · DOI · Paper page
- Vizcaíno, 2014, ProteomeXchange provides globally coordinated proteomics data submission and dissemination, Nature Biotechnology, 32, 223, 10.1038/nbt.2839 · DOI
- Waschbüsch, 2014, LRRK2 transport is regulated by its novel interacting partner Rab32, PLoS One, 9, e111632, 10.1371/journal.pone.0111632 · DOI
- Wiggin, 2002, MSK1 and MSK2 are required for the mitogen- and stress-induced phosphorylation of CREB and ATF1 in fibroblasts, Molecular and Cellular Biology, 22, 2871, 10.1128/MCB.22.8.2871-2881.2002 · DOI
- Wilson, 2014, Mutations in RAB39B cause X-linked intellectual disability and early-onset Parkinson disease with α-synuclein pathology, The American Journal of Human Genetics, 95, 729, 10.1016/j.ajhg.2014.10.015 · DOI
- Wu, 2005, Structural basis for recruitment of RILP by small GTPase Rab7, The EMBO Journal, 24, 1491, 10.1038/sj.emboj.7600643 · DOI
- Yoshimura, 2007, Functional dissection of Rab GTPases involved in primary cilium formation, The Journal of Cell Biology, 178, 363, 10.1083/jcb.200703047 · DOI
- Zimprich, 2004, Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology, Neuron, 44, 601, 10.1016/j.neuron.2004.11.005 · DOI
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Metadata
- Authors
- Steger, M., Diez, F., Dhekne, H. S., Lis, P., Nirujogi, R. S., Karayel, O., Tonelli, F., Martinez, T. N., Lorentzen, E., Pfeffer, S. R., Alessi, D. R., & Mann, M.
- Venue
- eLife
- Publisher
- eLife Sciences Publications, Ltd
- Published
- 2017-11-10
- Volume
- 6
- ISSN
- 2050-084X
- PMC
- PMC5695910
- Cited by
- 482
- References
- 8
- Language
- en
- Licence
- Funders
- Max-Planck-Gesellschaft
- Michael J. Fox Foundation for Parkinson's Research (6986.05)
- Medical Research Council (357811350 R60)
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