Effects of three deafness-causing gamma-actin mutations on actin structure and function

2013 ◽  
Author(s):  
Karina Annette Kruth
Keyword(s):  
Structure And Function ◽  
Actin Structure ◽  
And Function

scholarly journals Actin Structure and Function: What We Still Do Not Understand

2007 ◽  
Vol 282 (50) ◽  
pp. 36133-36137 ◽  
Author(s):  
Emil Reisler ◽  
Edward H. Egelman
Keyword(s):  
Structure And Function ◽  
Actin Structure ◽  
And Function

scholarly journals A Comparison between Vanadyl, Vanadate, and Decavanadate Effects in Actin Structure and Function: Combination of Several Spectroscopic Studies

2012 ◽  
Vol 27 ◽  
pp. 355-359 ◽  
Author(s):  
S. Ramos ◽  
J. J. G. Moura ◽  
M. Aureliano
Keyword(s):  
Actin Polymerization ◽  
Hydrophobic Surface ◽  
Spectroscopic Studies ◽  
Structure And Function ◽  
Actin Binding ◽  
Cysteine Oxidation ◽  
Natural Ligand ◽  
Function Combination ◽  
Actin Structure ◽  
And Function

The studies about the interaction of actin with vanadium are seldom. In the present paper the effects of vanadyl, vanadate, and decavanadate in the actin structure and function were compared. Decavanadate clearly interacts with actin, as shown byV51-NMR spectroscopy. Decavanadate interaction with actin induces protein cysteine oxidation and vanadyl formation, being both prevented by the natural ligand of the protein, ATP. Monomeric actin (G-actin) titration with vanadyl, as analysed by EPR spectroscopy, indicates a 1 : 1 binding stoichiometry and akdof 7.5 μM. Both decavanadate and vanadyl inhibited G-actin polymerization into actin filaments (F-actin), with aIC50of 68 and 300 μM, respectively, as analysed by light-scattering assays. However, only vanadyl induces G-actin intrinsic fluorescence quenching, which suggests the presence of vanadyl high-affinity actin-binding sites. Decavanadate increases (2.6-fold) actin hydrophobic surface, evaluated using the ANSA probe, whereas vanadyl decreases it (15%). Finally, both vanadium species increasedε-ATP exchange rate (k=6.5×10−3and4.47×10−3 s−1for decavanadate and vanadyl, resp.). Putting it all together, it is suggested that actin, which is involved in many cellular processes, might be a potential target not only for decavanadate but above all for vanadyl.

scholarly journals Arp2/3 complex-deficient mouse fibroblasts are viable and have normal leading-edge actin structure and function

2005 ◽  
Vol 102 (45) ◽  
pp. 16263-16268 ◽  
Author(s):  
A. Di Nardo ◽  
G. Cicchetti ◽  
H. Falet ◽  
J. H. Hartwig ◽  
T. P. Stossel ◽  
...  
Keyword(s):  
Leading Edge ◽  
Structure And Function ◽  
Deficient Mouse ◽  
Mouse Fibroblasts ◽  
Actin Structure ◽  
And Function

scholarly journals Structure and Mechanism of Mouse Cyclase-associated Protein (CAP1) in Regulating Actin Dynamics

2014 ◽  
Vol 289 (44) ◽  
pp. 30732-30742 ◽  
Author(s):  
Silvia Jansen ◽  
Agnieszka Collins ◽  
Leslie Golden ◽  
Olga Sokolova ◽  
Bruce L. Goode
Keyword(s):  
Plant Species ◽  
Structure And Function ◽  
Actin Dynamics ◽  
Actin Binding ◽  
Nucleotide Exchange ◽  
Actin Turnover ◽  
Actin Structure ◽  
Wh2 Domain ◽  
And Function ◽  
Β Sheet

Srv2/CAP is a conserved actin-binding protein with important roles in driving cellular actin dynamics in diverse animal, fungal, and plant species. However, there have been conflicting reports about whether the activities of Srv2/CAP are conserved, particularly between yeast and mammalian homologs. Yeast Srv2 has two distinct functions in actin turnover: its hexameric N-terminal-half enhances cofilin-mediated severing of filaments, while its C-terminal-half catalyzes dissociation of cofilin from ADP-actin monomers and stimulates nucleotide exchange. Here, we dissected the structure and function of mouse CAP1 to better understand its mechanistic relationship to yeast Srv2. Although CAP1 has a shorter N-terminal oligomerization sequence compared with Srv2, we find that the N-terminal-half of CAP1 (N-CAP1) forms hexameric structures with six protrusions, similar to N-Srv2. Further, N-CAP1 autonomously binds to F-actin and decorates the sides and ends of filaments, altering F-actin structure and enhancing cofilin-mediated severing. These activities depend on conserved surface residues on the helical-folded domain. Moreover, N-CAP1 enhances yeast cofilin-mediated severing, and conversely, yeast N-Srv2 enhances human cofilin-mediated severing, highlighting the mechanistic conservation between yeast and mammals. Further, we demonstrate that the C-terminal actin-binding β-sheet domain of CAP1 is sufficient to catalyze nucleotide-exchange of ADP-actin monomers, while in the presence of cofilin this activity additionally requires the WH2 domain. Thus, the structures, activities, and mechanisms of mouse and yeast Srv2/CAP homologs are remarkably well conserved, suggesting that the same activities and mechanisms underlie many of the diverse actin-based functions ascribed to Srv2/CAP homologs in different organisms.

scholarly journals Actin Structure and Function

2011 ◽  
Vol 40 (1) ◽  
pp. 169-186 ◽  
Author(s):  
Roberto Dominguez ◽  
Kenneth C. Holmes
Keyword(s):  
Structure And Function ◽  
Actin Structure ◽  
And Function

scholarly journals Modulation of actin structure and function by phosphorylation of Tyr-53 and profilin binding

2008 ◽  
Vol 105 (33) ◽  
pp. 11748-11753 ◽  
Author(s):  
K. Baek ◽  
X. Liu ◽  
F. Ferron ◽  
S. Shu ◽  
E. D. Korn ◽  
...  
Keyword(s):  
Structure And Function ◽  
Actin Structure ◽  
And Function

Structure and function of neural networks in the retina

1988 ◽  
Vol 46 ◽  
pp. 26-27
Author(s):  
Peter Sterling
Keyword(s):  
Ganglion Cells ◽  
Three Dimensional ◽  
Structure And Function ◽  
Synaptic Connections ◽  
Visual Axis ◽  
One Dimensional ◽  
Cat Retina ◽  
Ultrathin Sections ◽  
And Function ◽  
Insight Into

The synaptic connections in cat retina that link photoreceptors to ganglion cells have been analyzed quantitatively. Our approach has been to prepare serial, ultrathin sections and photograph en montage at low magnification (˜2000X) in the electron microscope. Six series, 100-300 sections long, have been prepared over the last decade. They derive from different cats but always from the same region of retina, about one degree from the center of the visual axis. The material has been analyzed by reconstructing adjacent neurons in each array and then identifying systematically the synaptic connections between arrays. Most reconstructions were done manually by tracing the outlines of processes in successive sections onto acetate sheets aligned on a cartoonist's jig. The tracings were then digitized, stacked by computer, and printed with the hidden lines removed. The results have provided rather than the usual one-dimensional account of pathways, a three-dimensional account of circuits. From this has emerged insight into the functional architecture.

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