Author

C. P. Johnson

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· 2 Biophysics· 1

Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 2 Approach:experimental assay· 2 Organism:yeast· 2 Research Focus:protein folding & dynamics· 1 Approach:statistical model· 1

Frequent Co-Authors

J. B. Kelley· 2 shared A. Hart· 1 shared A. J. Hart· 1 shared A. Khalil· 1 shared C. J. Kuykendall· 1 shared K. F. Jarvis· 1 shared L. E. Genrich· 1 shared M. Scandura· 1 shared

Activity by Year

2021-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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2 shared papersCell Biology

J. B. Kelley

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Author profile →

3 papers

Recent·Most cited

Septin Organization is Regulated by the Gpa1 Ubiquitination Domain and Endocytic Machinery During the Yeast Pheromone Response.

C. P. Johnson, S. Shrestha, A. Hart, K. F. Jarvis, L. E. Genrich, S. G. Latario, N. Leclerc, R. P. Geohegan, M. Scandura, T. Systuk, A. Khalil, J. B. Kelley

This study shows that Gpa1 ubiquitination and endocytic machinery regulate septin organization during yeast pheromone response by controlling their localization at the polarity site.

bioRxiv · Jun 16, 2023Cell Biology

Dynamic Phosphorylation of RGS Provides Spatial Regulation of MAP Kinase And Promotes Completion of Cytokinesis during the Yeast Pheromone Response

W. C. Simke, C. P. Johnson, A. J. Hart, S. Mayhue, P. L. Craig, S. Sojka, J. B. Kelley

The paper investigates how phosphorylation of the RGS Sst2 regulates MAP kinase localization and cytokinesis during the yeast pheromone response.

bioRxiv · Jun 22, 2021 · PreprintCell Biology

Calcium Sensitive Allostery Regulates the PI(4,5)P2 Binding Site of the Dysferlin C2A Domain

S. C. Otto, P. N. Reardon, T. M. Kumar, C. J. Kuykendall, C. P. Johnson

The paper identifies how calcium binding affects the dynamics of the dysferlin C2A domain's phosphoinositide binding site, revealing a mechanism for calcium-dependent membrane targeting.

bioRxiv · Feb 10, 2021 · PreprintBiophysics