Actin is a ubiquitous multifunctional protein that participates in cytoskeletal dynamics, cellular motility, intracellular signaling, and regulating gene expression, among other key cellular roles. Its functions rely critically upon the regulation of its polymerization. Although much is known about the structure and roles of filamentous actin (F-actin), the mechanisms by which actin nucleation occurs are still being elucidated.
A recent Cell paper revealed [url=Actin is a ubiquitous multifunctional protein that participates in cytoskeletal dynamics, cellular motility, intracellular signaling, and regulating gene expression, among other key cellular roles. Its functions rely critically upon the regulation of its polymerization. Although much is known about the structure and roles of filamentous actin (F-actin), the mechanisms by which actin nucleation occurs are still being elucidated.
A recent Cell paper revealed new insights into how actin nucleation occurs. The VopL effector protein binds three actin monomers at once and organizes them into a spatial arrangement close to that found in the canonical actin filament. Structural similarities with the more widely studied Arp2/3 complex and formin proteins suggest that this may be a general mechanism for actin nucleation.
This study used gene synthesis of native and mutant sequences encoding VopL-C-terminal domain peptides in order to obtain a crystal structure revealing how VopL binds to actin. Gene Synthesis from GenScript provides customized bioreagents for cell biology research, including investigations of:
cell cycle progression
cell polarity and cilia formation
neuronal filopodia formation
biosynthetic pathways that regulate cell metabolism
subcellular responses to reactive oxygen species
and the role of cytoskeletal elements in viral infection and parasitic invasion]new insights into how actin nucleation occurs[/url]. The VopL effector protein binds three actin monomers at once and organizes them into a spatial arrangement close to that found in the canonical actin filament. Structural similarities with the more widely studied Arp2/3 complex and formin proteins suggest that this may be a general mechanism for actin nucleation.
This study used gene synthesis of native and mutant sequences encoding VopL-C-terminal domain peptides in order to obtain a crystal structure revealing how VopL binds to actin. Gene Synthesis from GenScript provides customized bioreagents for cell biology research, including investigations of:
cell cycle progression
cell polarity and cilia formation
neuronal filopodia formation
biosynthetic pathways that regulate cell metabolism
subcellular responses to reactive oxygen species
and the role of cytoskeletal elements in viral infection and parasitic invasion
A recent Cell paper revealed [url=Actin is a ubiquitous multifunctional protein that participates in cytoskeletal dynamics, cellular motility, intracellular signaling, and regulating gene expression, among other key cellular roles. Its functions rely critically upon the regulation of its polymerization. Although much is known about the structure and roles of filamentous actin (F-actin), the mechanisms by which actin nucleation occurs are still being elucidated.
A recent Cell paper revealed new insights into how actin nucleation occurs. The VopL effector protein binds three actin monomers at once and organizes them into a spatial arrangement close to that found in the canonical actin filament. Structural similarities with the more widely studied Arp2/3 complex and formin proteins suggest that this may be a general mechanism for actin nucleation.
This study used gene synthesis of native and mutant sequences encoding VopL-C-terminal domain peptides in order to obtain a crystal structure revealing how VopL binds to actin. Gene Synthesis from GenScript provides customized bioreagents for cell biology research, including investigations of:
cell cycle progression
cell polarity and cilia formation
neuronal filopodia formation
biosynthetic pathways that regulate cell metabolism
subcellular responses to reactive oxygen species
and the role of cytoskeletal elements in viral infection and parasitic invasion]new insights into how actin nucleation occurs[/url]. The VopL effector protein binds three actin monomers at once and organizes them into a spatial arrangement close to that found in the canonical actin filament. Structural similarities with the more widely studied Arp2/3 complex and formin proteins suggest that this may be a general mechanism for actin nucleation.
This study used gene synthesis of native and mutant sequences encoding VopL-C-terminal domain peptides in order to obtain a crystal structure revealing how VopL binds to actin. Gene Synthesis from GenScript provides customized bioreagents for cell biology research, including investigations of:
cell cycle progression
cell polarity and cilia formation
neuronal filopodia formation
biosynthetic pathways that regulate cell metabolism
subcellular responses to reactive oxygen species
and the role of cytoskeletal elements in viral infection and parasitic invasion