T
Travis L. Rodkey
Researcher at University of Texas Health Science Center at Houston
Publications - 5
Citations - 392
Travis L. Rodkey is an academic researcher from University of Texas Health Science Center at Houston. The author has contributed to research in topics: Lipid bilayer fusion & Signal transduction. The author has an hindex of 5, co-authored 5 publications receiving 347 citations. Previous affiliations of Travis L. Rodkey include University of Texas at Austin & Rice University.
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Journal ArticleDOI
Signal integration by lipid-mediated spatial cross talk between Ras nanoclusters.
TL;DR: It is concluded that phosphatidylserine maintains the lateral segregation of diverse lipid-based assemblies on the plasma membrane and that lateral connectivity between spatially remote lipid assemblies offers important previously unexplored opportunities for signal integration and signal processing.
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Caveolae regulate the nanoscale organization of the plasma membrane to remotely control Ras signaling
Nicholas Ariotti,Manuel A. Fernandez-Rojo,Yong Zhou,Michelle M. Hill,Travis L. Rodkey,Kerry L. Inder,Lukas B. Tanner,Markus R. Wenk,John F. Hancock,Robert G. Parton +9 more
TL;DR: Caveolae transduce mechanical stress into plasma membrane lipid alterations that disrupt Ras organization in an isoform-specific manner and modulate downstream signal transduction.
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Another surprise from Metformin: novel mechanism of action via K-Ras influences endometrial cancer response to therapy
David A. Iglesias,Melinda S. Yates,Dharini van der Hoeven,Travis L. Rodkey,Qian Zhang,Ngai Na Co,Jennifer K. Burzawa,Sravanthi Chigurupati,Joseph Celestino,Jessica L. Bowser,Russell Broaddus,John F. Hancock,Rosemarie Schmandt,Karen H. Lu +13 more
TL;DR: Metformin inhibited cell proliferation, induced apoptosis, and decreased tumor growth in preclinical endometrial cancer models, with the greatest response observed in cells harboring activating mutations in K-Ras, revealing a novel mechanism of action for metformin.
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Munc18a Scaffolds SNARE Assembly to Promote Membrane Fusion
TL;DR: In vitro fusion assays suggest that Munc18a binds to the Syntaxin1a NRD and H3 domain within the assembled t-SNARE complex, positioning them for productive VAMP2 binding.
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The polybasic juxtamembrane region of Sso1p is required for SNARE function in vivo.
TL;DR: The results suggest that the sequence of the juxtamembrane region of Sso1p is vital for function in vivo, independent of the ability of these proteins to direct membrane fusion.