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The Roc domain of leucine-rich repeat kinase 2 is sufficient for interaction with microtubules
Journal of neuroscience research, 2008-06, Vol.86 (8), p.1711-1720
Gandhi, Payal N.
Wang, Xinglong
Zhu, Xiongwei
Chen, Shu G.
Wilson-Delfosse, Amy L.
2008
Details
Autor(en) / Beteiligte
Gandhi, Payal N.
Wang, Xinglong
Zhu, Xiongwei
Chen, Shu G.
Wilson-Delfosse, Amy L.
Titel
The Roc domain of leucine-rich repeat kinase 2 is sufficient for interaction with microtubules
Ist Teil von
Journal of neuroscience research, 2008-06, Vol.86 (8), p.1711-1720
Ort / Verlag
Hoboken: Wiley Subscription Services, Inc., A Wiley Company
Erscheinungsjahr
2008
Link zum Volltext
Quelle
Wiley Online Library Journals Frontfile Complete
Beschreibungen/Notizen
Mutations in the leucine‐rich repeat kinase 2 (LRRK2) gene are the leading cause of genetically inherited Parkinson's disease (PD). Although this multidomain protein has been shown to have both GTPase and kinase activities through the Roc and MAPKKK domains, respectively, the protein–protein interactions and pathways involved in LRRK2‐mediated signaling remain elusive. Utilizing a combination of protein pull‐down assays, mass spectrometry, Western blotting, and immunofluorescence microscopy, this study identifies and describes the interaction between LRRK2 and microtubules. The Roc or GTPase‐like domain of LRRK2 is sufficient for interaction with α/β‐tubulin heterodimers. This interaction occurs in a guanine nucleotide‐independent manner, suggesting that tubulin might not be an effector of the LRRK2 GTPase domain. The R1441C pathogenic mutation, located within the Roc domain, retains interaction with α/β‐tubulin heterodimers, suggesting that disruption of this interaction likely is not the mechanism whereby the R1441C mutation leads to disease. At a subcellular level, endogenous LRRK2 protein was found to colocalize with α/β‐tubulin in primary hippocampal neurons. These findings are significant in that they link LRRK2 with microtubules, a structural component of the cell that is critically involved in the pathogenesis of several neurodegenerative diseases, including PD. © 2008 Wiley‐Liss, Inc.
Sprache
Englisch
Identifikatoren
ISSN: 0360-4012
eISSN: 1097-4547
DOI: 10.1002/jnr.21622
Titel-ID: cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2586915
Format
–
Schlagworte
Amino Acid Sequence
,
Animals
,
Cell Line
,
GTP Phosphohydrolases - genetics
,
GTP Phosphohydrolases - metabolism
,
Humans
,
leucine-rich repeat kinase 2
,
Leucine-Rich Repeat Serine-Threonine Protein Kinase-2
,
Mice
,
Microtubules - genetics
,
Microtubules - physiology
,
Molecular Sequence Data
,
Mutation
,
neurodegeneration
,
NIH 3T3 Cells
,
Parkinson Disease - enzymology
,
Parkinson Disease - pathology
,
Parkinson's disease
,
Protein Structure, Tertiary - physiology
,
Protein-Serine-Threonine Kinases - genetics
,
Protein-Serine-Threonine Kinases - physiology
,
R1441C
,
tubulin
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