T
Thomas A. Masters
Researcher at University of Cambridge
Publications - 16
Citations - 993
Thomas A. Masters is an academic researcher from University of Cambridge. The author has contributed to research in topics: Actin & Myosin. The author has an hindex of 12, co-authored 16 publications receiving 846 citations. Previous affiliations of Thomas A. Masters include University College London & London Research Institute.
Papers
More filters
Journal ArticleDOI
Mechanical feedback between membrane tension and dynamics
TL;DR: The importance of membrane area and of tension as a master integrator of cell functions, particularly for membrane traffic, is discussed.
Journal ArticleDOI
Plasma membrane tension orchestrates membrane trafficking, cytoskeletal remodeling, and biochemical signaling during phagocytosis
TL;DR: It is proposed that, during phagocytosis, membrane remodeling, cytoskeletal organization, and biochemical signaling are orchestrated by the mechanical signal of membrane tension, which put a simple mechanical signal at the heart of understanding immunological responses.
Journal ArticleDOI
Evidence for a fence that impedes the diffusion of phosphatidylinositol 4,5-bisphosphate out of the forming phagosomes of macrophages
Urszula Golebiewska,Jason G. Kay,Thomas A. Masters,Sergio Grinstein,Wonpil Im,Richard W. Pastor,Suzanne Scarlata,Stuart McLaughlin,Stuart McLaughlin +8 more
TL;DR: Fluorescence correlation spectroscopy and fluorescence recovery after photobleaching measurements on macrophages injected with fluorescent phosphatidylinositol 4,5-bisphosphate suggest that a barrier impedes the diffusion of plasma membrane PIP2 into and out of forming phagosomes.
Journal ArticleDOI
Myosin VI-Dependent Actin Cages Encapsulate Parkin-Positive Damaged Mitochondria
Antonina J. Kruppa,Chieko Kishi-Itakura,Thomas A. Masters,Joanna Rorbach,Guinevere L. Grice,John Kendrick-Jones,James A. Nathan,Michal Minczuk,Folma Buss +8 more
TL;DR: It is demonstrated that MYO6 (myosin VI), a unique myosin that moves toward the minus end of actin filaments, forms a complex with Parkin and is selectively recruited to damaged mitochondria via its ubiquitin-binding domain.
Journal ArticleDOI
Regulation of 3-Phosphoinositide–Dependent Protein Kinase 1 Activity by Homodimerization in Live Cells
Thomas A. Masters,Thomas A. Masters,Véronique Calleja,D. A. Armoogum,Richard J. Marsh,Christopher J. Applebee,Michel Laguerre,Angus J. Bain,Banafshé Larijani +8 more
TL;DR: It is found that homodimerization of PDK1 is a spatially and temporally regulated mechanism for controlling PDK2 activity and offers possibilities for controllingPDK1 activity therapeutically.