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Rab10 Phosphorylation is a Prominent Pathological Feature in Alzheimer’s Disease

Yan, Tingxiang, Wang, Luwen, Gao, Ju, Siedlak, Sandra L., Huntley, Mikayla L., Termsarasab, Pichet, Perry, George, Chen, Shu G., Wang, Xinglong·2018·Journal of Alzheimer's Disease
DOI 10.3233/jad-180023PMC PMC6008156
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Crossref · 10.3233/jad-180023

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  • Rab10 likely plays a role in neurodegenerative diseases including Parkinson's and Alzheimer's diseases.

    “Rab10 and its phosphorylated form, pRab10 likely play a role in neurodegenerative diseases including Parkinson’s and Alzheimer’s diseases [64, 79, 94].”

    From Cellular and subcellular localization of Rab10 and phospho-T73 Rab10 in the mouse and human brain (2023) · cites this paper as [94]

    The Discussion (page unavailable) argues for an important role of Rab10 in Alzheimer’s disease and suggests pathological significance for Rab10 phosphorylation there. The Introduction (page unavailable) links Rab10 phosphorylation to LRRK2, a Parkinson’s-associated kinase, but does not say that Rab10 or pRab10 likely plays a role in Parkinson’s disease. (LLM, conf=0.82)

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  • pRab10 likely plays a role in neurodegenerative diseases including Parkinson's and Alzheimer's diseases.

    “Rab10 and its phosphorylated form, pRab10 likely play a role in neurodegenerative diseases including Parkinson’s and Alzheimer’s diseases [64, 79, 94].”

    From Cellular and subcellular localization of Rab10 and phospho-T73 Rab10 in the mouse and human brain (2023) · cites this paper as [94]

    The Discussion (page not available) identifies pRab10 as a prominent feature of Alzheimer’s disease and suggests it may contribute to disease-related changes. The Introduction (page not available) links Rab10 phosphorylation to LRRK2, a kinase associated with Parkinson’s disease, but does not establish that pRab10 plays a role in Parkinson’s disease. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

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Research works printed but not linked: 35

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  6. Chen, 2006, RAB-10 is required for endocytic recycling in the Caenorhabditis elegans intestine, Mol Biol Cell, 17, 1286, 10.1091/mbc.e05-08-0787 · DOI · Paper page
  7. Chen, 2012, Rab10 and myosin-Va mediate insulin-stimulated GLUT4 storage vesicle translocation in adipocytes, J Cell Biol, 198, 545, 10.1083/jcb.201111091 · DOI
  8. Wang, 2010, Ras-related protein Rab10 facilitates TLR4 signaling by promoting replenishment of TLR4 onto the plasma membrane, Proc Natl Acad Sci U S A, 107, 13806, 10.1073/pnas.1009428107 · DOI · Paper page
  9. Glodowski, 2007, RAB-10 regulates glutamate receptor recycling in a cholesterol-dependent endocytosis pathway, Mol Biol Cell, 18, 4387, 10.1091/mbc.e07-05-0486 · DOI · Paper page
  10. Wang, 2011, Lgl1 activation of rab10 promotes axonal membrane trafficking underlying neuronal polarization, Dev Cell, 21, 431, 10.1016/j.devcel.2011.07.007 · DOI
  11. Schuck, 2007, Rab10 is involved in basolateral transport in polarized madin-darby canine kidney cells, Traffic, 8, 47, 10.1111/j.1600-0854.2006.00506.x · DOI · Paper page
  12. Taylor, 2015, RAB-10 regulates dendritic branching by balancing dendritic transport, PLoS Genet, 11, e1005695, 10.1371/journal.pgen.1005695 · DOI
  13. Zou, 2015, RAB-10-dependent membrane transport is required for dendrite arborization, PLoS Genet, 11, e1005484, 10.1371/journal.pgen.1005484 · DOI
  14. Fan, 2018, Interrogating Parkinson’s disease LRRK2 kinase pathway activity by assessing Rab10 phosphorylation in human neutrophils, Biochem J, 475, 23, 10.1042/BCJ20170803 · DOI · Paper page
  15. Thirstrup, 2017, Selective LRRK2 kinase inhibition reduces phosphorylation of endogenous Rab10 and Rab12 in human peripheral mononuclear blood cells, Sci Rep, 7, 10300, 10.1038/s41598-017-10501-z · DOI
  16. 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
  17. Ito, 2016, Phos-tag analysis of Rab10 phosphorylation by LRRK2: A powerful assay for assessing kinase function and inhibitors, Biochem J, 473, 2671, 10.1042/BCJ20160557 · DOI · Paper page
  18. Zhu, 2000, Activation of p38 kinase links tau phosphorylation, oxidative stress, and cell cycle-related events in Alzheimer disease, J Neuropathol Exp Neurol, 59, 880, 10.1093/jnen/59.10.880 · DOI · Paper page
  19. Nunomura, 1999, RNA oxidation is a prominent feature of vulnerable neurons in Alzheimer’s disease, J Neurosci, 19, 1959, 10.1523/JNEUROSCI.19-06-01959.1999 · DOI
  20. Yao, 2004, Synaptic frailty and clathrin-mediated synaptic vesicle trafficking in Alzheimer’s disease, Trends Neurosci, 27, 24, 10.1016/j.tins.2003.10.012 · DOI
  21. Coleman, 2004, A focus on the synapse for neuroprotection in Alzheimer disease and other dementias, Neurology, 63, 1155, 10.1212/01.WNL.0000140626.48118.0A · DOI · Paper page
  22. Terry, 1991, Physical basis of cognitive alterations in Alzheimer’s disease: Synapse loss is the major correlate of cognitive impairment, Ann Neurol, 30, 572, 10.1002/ana.410300410 · DOI · Paper page
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Metadata

Authors
Yan, T., Wang, L., Gao, J., Siedlak, S. L., Huntley, M. L., Termsarasab, P., Perry, G., Chen, S. G., & Wang, X.
Venue
Journal of Alzheimer's Disease
Publisher
SAGE Publications
Published
2018-04-10
Volume
63
Issue
1
Pages
157-165
ISSN
  • 1387-2877
  • 1875-8908
DOI
10.3233/jad-180023
PMC
PMC6008156
Cited by
42
References
3

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