Results 21 to 30 of about 3,184,320 (288)
The budding yeast Saccharomyces cerevisiae has an actin cytoskeleton that comprises a set of protein components analogous to those found in the actin cytoskeletons of higher eukaryotes. Furthermore, the actin cytoskeletons of S.
Zain Akram +8 more
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Summary: Membrane curvature has emerged as an intriguing physical principle underlying biological signaling and membrane trafficking. The CIP4/FBP17/Toca-1 F-BAR subfamily is unique in the BAR family because its structurally folded F-BAR domain does not ...
Maohan Su +6 more
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The F-BAR domain is emerging as an important player in membrane remodeling pathways. F-BAR domain proteins couple membrane remodeling with actin dynamics associated with endocytic pathways and filopodium formation. Here, we provide a comprehensive analysis of F-BAR domain proteins in terms of their evolutionary relationships and protein function. F-BAR
Sohail, Ahmed +4 more
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Polarized hyphal growth of filamentous pathogenic fungi is an essential event for host penetration and colonization. The long-range early endosomal trafficking during hyphal growth is crucial for nutrient uptake, sensing of host-specific cues, and ...
Manisha Sinha +6 more
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Membrane sculpting by F-BAR domains studied by molecular dynamics simulations. [PDF]
Interplay between cellular membranes and their peripheral proteins drives many processes in eukaryotic cells. Proteins of the Bin/Amphiphysin/Rvs (BAR) domain family, in particular, play a role in cellular morphogenesis, for example curving planar ...
Hang Yu, Klaus Schulten
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Membrane-Sculpting BAR Domains Generate Stable Lipid Microdomains
Bin-Amphiphysin-Rvs (BAR) domain proteins are central regulators of many cellular processes involving membrane dynamics. BAR domains sculpt phosphoinositide-rich membranes to generate membrane protrusions or invaginations.
Hongxia Zhao +6 more
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Membrane Binding by the Endophilin N-BAR Domain [PDF]
The structure of the endophilin N-terminal amphipathic helix Bin/Amphiphysin/Rvs-homology (N-BAR) domain is unique because of an additional insert helix under the arch of the N-BAR dimer. The structure of this additional helix has not been fully resolved in crystallographic studies, and thus presents a challenge to molecular-level analysis. Large-scale
Cui, Haosheng +2 more
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Control of Rho GTPase function by BAR-domains [PDF]
Cytoskeletal dynamics are key to the establishment of cell polarity and the consequent coordination of protrusion and contraction that drives cell migration. During these events, the actin and microtubule cytoskeleton act in concert with the cellular machinery that controls endo-and exocytosis, thus regulating polarized traffic of membranes and ...
de Kreuk, Bart-Jan, Hordijk, Peter L.
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Versatile membrane deformation potential of activated pacsin. [PDF]
Endocytosis is a fundamental process in signaling and membrane trafficking. The formation of vesicles at the plasma membrane is mediated by the G protein dynamin that catalyzes the final fission step, the actin cytoskeleton, and proteins that sense or ...
Shih Lin Goh +3 more
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CryoEM reveals BIN1 (isoform 8) does not bind to single actin filaments in vitro
Cells change their appearance by a concerted action of the cytoskeleton and the plasma membrane. The machinery that bends the membrane includes Bin/Amphiphysin/Rvs (BAR) domain proteins. Recently BAR domain proteins garnered attention as actin regulators,
Zuoneng Wang, Carsten Mim
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