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Advances in elucidating the function of leucine-rich repeat protein kinase-2 in normal cells and Parkinson's disease
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Several RABs identified as being controlled by Retromer are substrates for LRRK2-mediated phosphorylation in response to disrupted lysosomal homoeostasis.
“several RABs identified as being controlled by Retromer are substrates for LRKK2-mediated phosphorylation in response to disrupted lysosomal homoeostasis127–129.”
From Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation (2025) · cites this paper as [128]
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RETRACTED ARTICLE: LRRK2 kinase regulates α-synuclein propagation via RAB35 phosphorylation
Bae, E.-J., Kim, D.-K., Kim, C., Mante, M., Adame, A., Rockenstein, E., Ulusoy, A., Klinkenberg, M., Jeong, G. R., Bae, J. R., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05958-z · Cited by 149
RetractedRab 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
Hui, K. Y., Fernandez-Hernandez, H., Hu, J., Schaffner, A., Pankratz, N., Hsu, N.-Y., Chuang, L.-S., Carmi, S., Villaverde, N., Li, X., et al. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aai7795 · Cited by 384
LRRK2 levels in immune cells are increased in Parkinson’s disease
Cook, D. A., Kannarkat, G. T., Cintron, A. F., Butkovich, L. M., Fraser, K. B., Chang, J., Grigoryan, N., Factor, S. A., West, A. B., Boss, J. M., et al. (2017) · npj Parkinson's Disease · doi:10.1038/s41531-017-0010-8 · Cited by 279
Dhekne, H. S., Yanatori, I., Gomez, R. C., Tonelli, F., Diez, F., Schüle, B., Steger, M., Alessi, D. R., & Pfeffer, S. R. (2018) · eLife · doi:10.7554/elife.40202 · Cited by 240
Self-citationHenry, A. G., Aghamohammadzadeh, S., Samaroo, H., Chen, Y., Mou, K., Needle, E., & Hirst, W. D. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv314 · Cited by 235
Takagawa, T., Kitani, A., Fuss, I., Levine, B., Brant, S. R., Peter, I., Tajima, M., Nakamura, S., & Strober, W. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aan8162 · Cited by 145
Lrrk2 alleles modulate inflammation during microbial infection of mice in a sex-dependent manner
Shutinoski, B., Hakimi, M., Harmsen, I. E., Lunn, M., Rocha, J., Lengacher, N., Zhou, Y. Y., Khan, J., Nguyen, A., Hake-Volling, Q., et al. (2019) · Science Translational Medicine · doi:10.1126/scitranslmed.aas9292 · Cited by 96
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Cited by
Sorted by citations
Kalogeropulou, A. F., Purlyte, E., Tonelli, F., Lange, S. M., Wightman, M., Prescott, A. R., Padmanabhan, S., Sammler, E., & Alessi, D. R. (2022) · Biochemical Journal · doi:10.1042/bcj20220161 · Cited by 129
Self-citationMapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation
Antón-Plágaro, C., Chen, K.-E., Guo, Q., Liu, M., Evans, A. J., Lewis, P. A., Heesom, K. J., Wilkinson, K. A., Collins, B. M., & Cullen, P. J. (2025) · Nature Communications · doi:10.1038/s41467-025-61802-1 · Cited by 14
Protein kinase inhibitors as therapeutics in neurodegenerative and psychiatric disorders
Tridente, G., Jana, A., Nath, A., & Ashraf, G. M. (2023) · Receptor Tyrosine Kinases in Neurodegenerative and Psychiatric Disorders · doi:10.1016/b978-0-443-18677-6.00015-4 · Cited by 8
Metadata
- Authors
- Taylor, M., & Alessi, D. R.
- ORCID
- Taylor, Matthew
- Venue
- Current Opinion in Cell Biology
- Publisher
- Elsevier BV
- Published
- 2020-04
- Volume
- 63
- Pages
- 102-113
- ISSN
- 0955-0674
- PMC
- PMC7262585
- Cited by
- 141
- References
- 8
- Language
- en
- Licence
- Funders
- GlaxoSmithKline
- Michael J. Fox Foundation for Parkinson's Research (17298 & 6986)
- Merck KGaA
- Stanford University
- Medical Research Council (MC_UU_12016/2)
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