R
Rebekah DeVinney
Researcher at University of British Columbia
Publications - 15
Citations - 2624
Rebekah DeVinney is an academic researcher from University of British Columbia. The author has contributed to research in topics: Intimin & Actin nucleation. The author has an hindex of 11, co-authored 15 publications receiving 2571 citations. Previous affiliations of Rebekah DeVinney include University of Calgary.
Papers
More filters
Journal ArticleDOI
Enteropathogenic E. coli (EPEC) Transfers Its Receptor for Intimate Adherence into Mammalian Cells
Brendan Kenny,Rebekah DeVinney,Markus Stein,Dieter J. Reinscheid,Elizabeth A. Frey,B. Brett Finlay +5 more
TL;DR: It is demonstrated that Hp90 is actually a bacterial protein (Tir), to which this bacterial pathogen inserts its own receptor into mammalian cell surfaces, to which it then adheres to trigger additional host signaling events and actin nucleation.
Journal ArticleDOI
Enteropathogenic E. coli Tir binds Nck to initiate actin pedestal formation in host cells.
Samantha Gruenheid,Rebekah DeVinney,Rebekah DeVinney,Friedhelm Bladt,Danika L. Goosney,Sigal Gelkop,Gerald D. Gish,Tony Pawson,B. Brett Finlay +8 more
TL;DR: It is shown that tyrosine 474 of Tir directly binds the host-cell adaptor protein Nck, and that Nck is required for the recruitment of both neural Wiskott–Aldrich-syndrome protein (N-WASP) and the actin-related protein (Arp)2/3 complex to the EPEC pedestal, directly linking Tir to the cytoskeleton.
Journal ArticleDOI
Enterohemorrhagic Escherichia coli O157:H7 Produces Tir, Which Is Translocated to the Host Cell Membrane but Is Not Tyrosine Phosphorylated
Rebekah DeVinney,Markus Stein,Dieter J. Reinscheid,Akio Abe,Sharon Ruschkowski,B. Brett Finlay +5 more
TL;DR: It is demonstrated that EHEC produces a functional Tir that is inserted into host cell membranes, where it serves as an intimin receptor, however, unlike in EPEC, in EH EC Tir is not tyrosine phosphorylated yet plays a key role in both bacterial adherence to epithelial cells and pedestal formation.
Journal ArticleDOI
Enteropathogenic Escherichia coli translocated intimin receptor, Tir, requires a specific chaperone for stable secretion.
Akio Abe,Myriam de Grado,Richard A. Pfuetzner,Claudia Sánchez-SanMartı́n,Rebekah DeVinney,José L. Puente,José L. Puente,Natalie C. J. Strynadka,B. Brett Finlay +8 more
TL;DR: Results indicate that CesT is a Tir chaperone that may act as an anti‐degradation factor by specifically binding to its amino‐terminus, forming a multimeric stabilized complex.
Journal ArticleDOI
Enteropathogenic E. coli translocated intimin receptor, Tir, interacts directly with α-actinin
Danika L. Goosney,Rebekah DeVinney,Richard A. Pfuetzner,Elizabeth A. Frey,Natalie C. J. Strynadka,B. Brett Finlay +5 more
TL;DR: It is shown that Tir directly binds the cytoskeletal protein alpha-actinin, the first known direct linkage between extracellular EPEC, through the transmembrane protein Tir, to the host cell actin cytoskeleton via alpha- actinin.