Author

M. L. Starr

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· 4

Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 3 Approach:experimental assay· 3 Organism:yeast· 3 Research Focus:chromatin & epigenetic regulation· 1 Approach:genetic perturbation / CRISPR· 1

Frequent Co-Authors

R. A. Fratti· 4 shared A. Guo· 3 shared B. C. Jones· 3 shared G. E. Miner· 3 shared K. D. Sullivan· 3 shared L. R. Hurst· 2 shared A. Arango· 1 shared C. Zhang· 1 shared

Activity by Year

2018-2019 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 35 mutual co-author links

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4 shared papersBiochemistry

R. A. Fratti

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4 papers

Recent·Most cited

Copper Blocks V-ATPase Activity and SNARE Complex Formation to Inhibit Yeast Vacuole Fusion

G. E. Miner, K. D. Sullivan, C. Zhang, L. R. Hurst, M. L. Starr, D. A. Rivera-Kohr, B. C. Jones, A. Guo, R. A. Fratti

This study shows that copper inhibits yeast vacuole fusion by blocking SNARE complex formation and V-ATPase activity, with Cu2+ being the active species.

bioRxiv · May 2, 2019Biochemistry

Phosphatidylinositol 3,5-Bisphosphate regulates Ca2+ Transport During Yeast Vacuolar Fusion through Activation of the Ca2+ ATPase Pmc1

G. E. Miner, K. D. Sullivan, A. Guo, M. L. Starr, E. C. Ellis, B. C. Jones, R. A. Fratti

This study shows that PI(3,5)P2 regulates Ca2+ transport in yeast vacuoles by activating Pmc1 during fusion, opposing its role in fission.

bioRxiv · Feb 1, 2019Biochemistry

Phosphatidylinositol 3,5-Bisphosphate Regulates Yeast Vacuole Fusion at the Transition between trans-SNARE Complex Formation and Hemifusion

G. E. Miner, K. D. Sullivan, A. Guo, B. C. Jones, M. L. Starr, R. A. Fratti

This study shows that PI(3,5)P2 inhibits yeast vacuole fusion after SNARE complex formation and during hemifusion, acting as a molecular switch between fission and fusion.

bioRxiv · Aug 10, 2018Biochemistry

Phosphatidic acid inhibits SNARE priming by inducing conformational changes in Sec18 protomers

M. L. Starr, R. A. Sparks, L. R. Hurst, Z. Zhao, A. Arango, M. Lihan, J. L. Jenkins, E. Tajkhorshid, R. A. Fratti

This study shows phosphatidic acid (PA) inhibits SNARE priming by altering Sec18 conformation and stabilizing membrane-bound protomers.

bioRxiv · Jul 9, 2018Biochemistry