Author

C. Y. Chiang

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 2 Cell Biology· 1

Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 2 Research Focus:cell type annotation· 2 Approach:experimental assay· 2 Assay:proteomics· 2 Approach:genetic perturbation / CRISPR· 1 Organism:human· 1 Organism:mouse· 1

Frequent Co-Authors

H. S. Dhekne· 3 shared S. R. Pfeffer· 3 shared A. Adhikari· 2 shared C. Limouse· 2 shared D. R. Alessi· 2 shared E. Purlyte· 2 shared W. M. Yeshaw· 2 shared E. G. Vides· 1 shared

Activity by Year

2022-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 40 mutual co-author links

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3 shared papersBiochemistry

H. S. Dhekne

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Author profile →

3 papers

Recent·Most cited

Localization of PPM1H phosphatase tunes Parkinsons disease-linked LRRK2 kinase-mediated Rab GTPase phosphorylation and ciliogenesis

W. M. Yeshaw, A. Adhikari, C. Y. Chiang, H. S. Dhekne, P. S. Wawro, S. R. Pfeffer

This paper shows that PPM1H phosphatase localization affects its ability to dephosphorylate Rab GTPases, influencing ciliogenesis and membrane trafficking.

Proceedings of the National Academy of Sciences · Oct 27, 2023Peer-reviewedCell Biology

Genome-wide screen reveals Rab12 GTPase as a critical activator of pathogenic LRRK2 kinase

H. S. Dhekne, F. Tonelli, W. M. Yeshaw, C. Y. Chiang, C. Limouse, E. Jaimon, E. Purlyte, D. R. Alessi, S. R. Pfeffer

The paper identifies Rab12 as a critical activator of pathogenic LRRK2 kinase through a CRISPR-based screen and structural analysis.

bioRxiv · Feb 17, 2023Biochemistry

A Feed-forward Pathway Drives LRRK2 kinase Membrane Recruitment and Activation

E. G. Vides, A. Adhikari, C. Y. Chiang, P. Lis, E. Purlyte, C. Limouse, J. L. Shumate, E. S. Lasso, H. S. Dhekne, D. R. Alessi, S. R. Pfeffer

This study identifies two distinct binding sites on LRRK2 that mediate its membrane recruitment and activation through Rab GTPase interactions, revealing a feed-forward pathway for kinase activity regulation.

bioRxiv · Apr 25, 2022Biochemistry