Steven Z. Chou
YOU?
Author Swipe
View article: Publisher Correction: Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex
Publisher Correction: Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex Open
View article: Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex
Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex Open
Arp2/3 complex nucleates branched actin filaments for cell and organelle movements. Here we report a 2.7 Å resolution cryo-EM structure of the mature branch junction formed by S. pombe Arp2/3 complex that provides details about interaction…
View article: Cryo-EM structure of the bacterial effector protein SipA bound to F-actin reveals a unique mechanism for filament stabilization
Cryo-EM structure of the bacterial effector protein SipA bound to F-actin reveals a unique mechanism for filament stabilization Open
The bacterial pathogen Salmonella spp. modulates cellular processes by delivering effector proteins through its type III secretion systems. Among these effectors, SipA facilitates bacterial invasion and promotes intestinal inflammation. Th…
View article: Cryo-EM structures of both ends of the actin filament explain why the barbed end elongates faster than the pointed end
Cryo-EM structures of both ends of the actin filament explain why the barbed end elongates faster than the pointed end Open
Actin filament ends are the sites of subunit addition during elongation and subunit loss during depolymerization. Prior work established the kinetics and thermodynamics of the assembly reactions at both ends but not the structural basis of…
View article: Mechanism of actin filament branch formation by Arp2/3 complex revealed by a high-resolution cryo-EM structureof the branch junction
Mechanism of actin filament branch formation by Arp2/3 complex revealed by a high-resolution cryo-EM structureof the branch junction Open
We reconstructed the structure of actin filament branch junctions formed by fission yeast Arp2/3 complex at 3.5 Å resolution from images collected by electron cryo-microscopy. During specimen preparation, all of the actin subunits and Arp3…
View article: Cryo-electron microscopy structures of pyrene-labeled ADP-Pi- and ADP-actin filaments
Cryo-electron microscopy structures of pyrene-labeled ADP-Pi- and ADP-actin filaments Open
Since the fluorescent reagent N-(1-pyrene)iodoacetamide was first used to label skeletal muscle actin in 1981, the pyrene-labeled actin has become the most widely employed tool to measure the kinetics of actin polymerization and the intera…
View article: Structural basis for polarized elongation of actin filaments
Structural basis for polarized elongation of actin filaments Open
Significance Eukaryotic cells utilize actin filaments to move, change shape, divide, and transport cargo. Decades of experiments have established that actin filaments elongate and shorten significantly faster from one end than the other, b…
View article: Cryo-electron microscopy structures of pyrene-labeled ADP-P<sub>i</sub>- and ADP-actin filaments
Cryo-electron microscopy structures of pyrene-labeled ADP-P<sub>i</sub>- and ADP-actin filaments Open
We report high resolution cryo-electron microscopy structures of actin filaments with N-1-pyrene conjugated to cysteine 374 and either ADP (3.2 Å) or ADP-phosphate (3.0 Å) in the active site. Polymerization buries pyrene in a hydrophobic c…
View article: Structural basis for polarized elongation of actin filaments
Structural basis for polarized elongation of actin filaments Open
Actin filaments elongate and shorten much faster at their barbed end than their pointed end, but the molecular basis of this difference has not been understood. We use all-atom molecular dynamics simulations to investigate the properties o…
View article: Mechanism of actin polymerization revealed by cryo-EM structures of actin filaments with three different bound nucleotides
Mechanism of actin polymerization revealed by cryo-EM structures of actin filaments with three different bound nucleotides Open
We used cryo-electron microscopy (cryo-EM) to reconstruct actin filaments with bound AMPPNP (β,γ-imidoadenosine 5′-triphosphate, an ATP analog, resolution 3.1 Å), ADP-P i (ADP with inorganic phosphate, resolution 3.1 Å), or ADP (resolution…
View article: Conformational changes in Arp2/3 complex induced by ATP, WASp-VCA, and actin filaments
Conformational changes in Arp2/3 complex induced by ATP, WASp-VCA, and actin filaments Open
Significance Arp2/3 complex consists of actin-related proteins 2 and 3 with five other subunits. It forms actin filament branches under the regulation of ATP, actin monomers, actin filaments, and a nucleation-promoting factor (NPF). Here w…
View article: Mechanism of actin polymerization revealed by cryo-EM structures of actin filaments with three different bound nucleotides
Mechanism of actin polymerization revealed by cryo-EM structures of actin filaments with three different bound nucleotides Open
We used electron cryo-micrographs to reconstruct actin filaments with bound AMPPNP (β,γ-imidoadenosine 5’-triphosphate, an ATP analog), ADP-P i (ADP with inorganic phosphate) or ADP to resolutions of 3.4 Å, 3.4 Å and 3.6 Å. Subunits in the…
View article: Conformational changes in Arp2/3 complex induced by ATP, WASp-VCA and actin filaments
Conformational changes in Arp2/3 complex induced by ATP, WASp-VCA and actin filaments Open
We used fluorescence spectroscopy and electron microscopy to determine how binding of ATP, nucleation-promoting factors (NPF), actin monomers and actin filaments change the conformation of Arp2/3 complex during the process that nucleates a…