Author

S. R. Pfeffer

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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Cell Biology· 5 Biochemistry· 4

Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 6 Approach:experimental assay· 6 Research Focus:cell type annotation· 4 Organism:human· 4 Assay:proteomics· 4 Organism:mouse· 3 Research Focus:development & morphogenesis· 2 Research Focus:drug response / drug discovery· 2

Frequent Co-Authors

H. S. Dhekne· 6 shared D. R. Alessi· 4 shared C. Y. Chiang· 3 shared F. Tonelli· 3 shared P. S. Wawro· 3 shared Y. Sobu· 3 shared A. Adhikari· 2 shared A. Lu· 2 shared

Activity by Year

2019-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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6 shared papersCell Biology

H. S. Dhekne

Mutual co-authors in cluster

Author profile →

9 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

CRISPR screens for lipid regulators reveal a role for ER-bound SNX13 in lysosomal cholesterol export

A. Lu, F. Hsieh, C. Enrich, S. R. Pfeffer

Two CRISPR screens identify SNX13 as a negative regulator of lysosomal cholesterol export, revealing its role in modifying NPC1 function and lipid homeostasis.

bioRxiv · May 10, 2021Cell Biology

Pathogenic LRRK2 control of primary cilia and Hedgehog signaling in neurons and astrocytes of mouse brain

S. S. Khan, Y. Sobu, H. S. Dhekne, F. Tonelli, K. Berndsen, D. R. Alessi, S. R. Pfeffer

The paper shows that LRRK2 mutations and PPM1H loss cause cilia loss in neurons and astrocytes, disrupting Hedgehog signaling in the nigral-striatal pathway.

bioRxiv · Mar 2, 2021Cell Biology

LRRK2-phosphorylated Rab10 sequesters Myosin Va with RILPL2 during ciliogenesis blockade

I. Yanatori, H. S. Dhekne, E. G. Vides, Y. Sobu, F. Diez, S. R. Pfeffer

This study identifies LRRK2-phosphorylated Rab10 as a key factor in sequestering Myosin Va and RILPL2, blocking ciliogenesis in RPE cells.

bioRxiv · Apr 28, 2020Cell Biology

Pathogenic LRRK2 regulates ciliation probability upstream of Tau Tubulin kinase 2

Y. Sobu, P. S. Wawro, H. S. Dhekne, S. R. Pfeffer

This study shows that pathogenic LRRK2 mutations reduce ciliation probability by blocking TTBK2 recruitment to the mother centriole, leading to ciliary decapitation in response to serum addition.

bioRxiv · Apr 7, 2020Cell Biology

Inter-domain dynamics drive cholesterol transport by NPC1 and NPC1L1 proteins

P. Saha, J. L. Shumate, J. G. Caldwell, N. Elghobashi-Meinhardt, A. Lu, L. Zhang, N. Olsson, J. E. Elias, S. R. Pfeffer

The paper investigates the role of inter-domain dynamics in cholesterol transport by NPC1 and NPC1L1 proteins, showing that domain movement is essential and that Ezetimibe inhibits NPC1L1 by binding to multiple domains.

bioRxiv · Mar 26, 2020Biochemistry

PPM1H phosphatase counteracts LRRK2 signaling by selectively dephosphorylating Rab proteins

K. Berndsen, P. Lis, W. Yeshaw, P. S. Wawro, R. S. Nirujogi, M. Wightman, T. Macartney, M. Dorward, A. Knebel, F. Tonelli, S. R. Pfeffer, D. R. Alessi

This study identifies PPM1H as a phosphatase that counteracts LRRK2 signaling by dephosphorylating Rab proteins, suggesting it as a potential therapeutic target for Parkinson's disease.

bioRxiv · Jul 22, 2019Biochemistry