Author

S. M. Travis

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· 3 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:cell signaling & trafficking· 3 Research Focus:chromatin & epigenetic regulation· 2 Organism:Xenopus· 2 Research Focus:cell type annotation· 1 Research Focus:cell-cell communication· 1 Assay:cryo-EM· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

F. M. Hughson· 2 shared P. D. Jeffrey· 2 shared S. Petry· 2 shared A. E. Stanton· 1 shared B. P. Mahon· 1 shared B. Romer· 1 shared G. Ramirez-Arellano· 1 shared I.-M. Yu· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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2 shared papersBiochemistry

F. M. Hughson

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Author profile →

4 papers

Recent·Most cited

Structure of a Membrane Tethering Complex Incorporating Multiple SNAREs

K. A. DAmico, A. E. Stanton, J. D. Shirkey, S. M. Travis, P. D. Jeffrey, F. M. Hughson

The paper presents a cryo-EM structure of the Dsl1 membrane tethering complex bound to SNAREs, revealing structural similarities to the exocyst complex and suggesting common principles in MTC function.

bioRxiv · Jan 30, 2023Biochemistry

RanGTP regulates the augmin complex

J. Kraus, S. M. Travis, M. R. King, S. Petry

The paper shows that RanGTP directly regulates the augmin complex, which is a spindle assembly factor, to control branching microtubule nucleation during mitosis.

bioRxiv · Dec 23, 2022 · PreprintBiochemistry

The conserved centrosomal motif, γTuNA, forms a dimer that directly activates microtubule nucleation by the γ-tubulin ring complex (γTuRC).

M. J. Rale, B. Romer, B. P. Mahon, S. M. Travis, S. Petry

This study identifies γTuNA as a dimer that directly activates γTuRC to nucleate microtubules, opposing stathmin inhibition.

bioRxiv · Apr 11, 2022 · PreprintBiochemistry

Structural basis for the binding of SNAREs to the multisubunit tethering complex Dsl1

S. M. Travis, K. DAmico, I.-M. Yu, S. Hamid, G. Ramirez-Arellano, P. D. Jeffrey, F. M. Hughson

This paper determines the structural basis of Dsl1 complex binding to ER SNAREs, showing how it anchors the complex and positions SNARE motifs for assembly.

bioRxiv · Apr 7, 2020Cell Biology