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Capping proteins

Barbed-end-capping proteins (gelsolin and villin, 95 kD) attach to this specific end of the actin filament and inhibit the further addition of actin molecules. [Pg.23]

Pointed-end-capping proteins are acumentin (65 kD), spectrin (220-260 kD), and p-actinin (37 kD). They also regulate the length of actin filaments. [Pg.23]

Stress fibers are parallel bundles of actin filaments that develop in the cytoplasm of fibroblasts from the cortical actin network in response to mechanical tension. These often bind to the plasma membrane at focal contacts and, through transmembrane linker glycoproteins, to the extracellular matrix. Thus, actin filaments of stress fibers indirectly Join to the inner face of the plasma membrane through molecular assemblies of attachment proteins, which include an actin-capping protein, a-actinin, vinculin, and talin (Small, 1988). [Pg.27]

Weeds, A.G., Maciver, S.K. (1993). F-actin capping proteins. Curr. Opin. Cell Biol. 5, 63-69. [Pg.106]

Figure 2 The actin-ADP-ribosylating toxins, (a) Molecular mode of action. The actin-ADP-ribosylating toxins covalently transfer an ADP-ribose moiety from NAD+ onto Arg177 of G-actin in the cytosol of targeted cells. Mono-ADP-ribosylated G-actin acts as a capping protein and inhibits the assembly of nonmodified actin into filaments. Thus, actin polymerization is blocked at the fast-growing ends of actin filaments (plus or barbed ends) but not at the slow growing ends (minus or pointed ends). This effect ultimately increases the critical concentration necessary for actin polymerization and tends to depolymerize F-actin. Finally, all actin within an intoxicated cell becomes trapped as ADP-ribosylated G-actin. Figure 2 The actin-ADP-ribosylating toxins, (a) Molecular mode of action. The actin-ADP-ribosylating toxins covalently transfer an ADP-ribose moiety from NAD+ onto Arg177 of G-actin in the cytosol of targeted cells. Mono-ADP-ribosylated G-actin acts as a capping protein and inhibits the assembly of nonmodified actin into filaments. Thus, actin polymerization is blocked at the fast-growing ends of actin filaments (plus or barbed ends) but not at the slow growing ends (minus or pointed ends). This effect ultimately increases the critical concentration necessary for actin polymerization and tends to depolymerize F-actin. Finally, all actin within an intoxicated cell becomes trapped as ADP-ribosylated G-actin.
Macrophage invasion — the up-regulation of the macrophage mannose receptor, cathepsin S, and macrophage capping protein. Up-regulation of irramme response genes — overexpression of major histocompatibility complex (MHC) and IgG. [Pg.183]

Equation 15 can aid in designing gel fraction assays for differing tasks. In certain instances the gel fraction will vary in proportion to the amount of crosslinking protein. However, if, fyr example, the capping protein concentration is varied, (l-g) dg/de can change according to Equation 8a as the product of an exponential and inverse square power of... [Pg.230]

Suppose, for example, that capping protein is in excess and that capping is irreversible. Then, by Equations 7 and 18, we readily find that the time to gelation is given as... [Pg.231]

Generally, however, A depends implicitly on other network parameters. The dependencies can be assessed by investigating the slope of G as experimental conditigns are changed. For example, if capping is irreversible (k = 0), G varies with the amount of capping protein as (cf. Equation 24)... [Pg.232]

Figure 3. Critical concentration behavior of actin self-assembly. For the top diagram depicting the macroscopic critical concentration curve, one determines the total amount of polymerized actin by methods that measure the sum of addition and release processes occurring at both ends. Examples of such methods are sedimentation, light scattering, fluorescence assays with pyrene-labeled actin, and viscosity measurements. Forthe bottom curves, the polymerization behavior is typically determined by fluorescence assays conducted under conditions where one of the ends is blocked by the presence of molecules such as gelsolin (a barbed-end capping protein) or spectrin-band 4.1 -actin (a complex prepared from erythrocyte membranes, such that only barbed-end growth occurs). Note further that the barbed end (or (+)-end) has a lower critical concentration than the pointed end (or (-)-end). This differential stabilization requires the occurrence of ATP hydrolysis to supply the free energy that drives subunit addition to the (+)-end at the expense of the subunit loss from the (-)-end. Figure 3. Critical concentration behavior of actin self-assembly. For the top diagram depicting the macroscopic critical concentration curve, one determines the total amount of polymerized actin by methods that measure the sum of addition and release processes occurring at both ends. Examples of such methods are sedimentation, light scattering, fluorescence assays with pyrene-labeled actin, and viscosity measurements. Forthe bottom curves, the polymerization behavior is typically determined by fluorescence assays conducted under conditions where one of the ends is blocked by the presence of molecules such as gelsolin (a barbed-end capping protein) or spectrin-band 4.1 -actin (a complex prepared from erythrocyte membranes, such that only barbed-end growth occurs). Note further that the barbed end (or (+)-end) has a lower critical concentration than the pointed end (or (-)-end). This differential stabilization requires the occurrence of ATP hydrolysis to supply the free energy that drives subunit addition to the (+)-end at the expense of the subunit loss from the (-)-end.
Barbed-End Capping Protein Blocks Net Assembly at Barbed Ends of Filaments... [Pg.20]

We then see that the rate of elongation in the presence of a capping protein will be given by the following rate law ... [Pg.21]

Note that if a capping protein binds to monomeric actin, the capping protein will also be a monomer-sequestering agent. A good example of such behavior is profilin. See also ABM-1 ABM-2 Sequences inActin-Based Motors Actin-Based Bacterial Motility Actin Assembly Kinetics... [Pg.21]

A molecule that functions in conjunction with a protein apo-activator. The classical example is cAMP, the coactivator of the CAP protein in bacteria. [Pg.155]

ACTIN-BASED BACTERIAL MOTILITY ACTIN ASSEMBLY ASSAYS ACTIN ASSEMBLY KINETICS ACTIN FILAMENT CAPPING PROTEIN ACTIN FILAMENT SEVERING PROTEIN... [Pg.718]

ACTIN FILAMENT CAPPING PROTEIN Actin cross-linking/bundling,... [Pg.719]

Fig. 1.15. Bending of the DNA in the CAP protein-DNA complex. The CAP protein ( . coli) binds as a dimer to the two-fold symmetric operator sequence. The DNA is bent nearly 90deg in the complex. The turns are centered around two GT sequences (shown in black) of the recognition element. Fig. 1.15. Bending of the DNA in the CAP protein-DNA complex. The CAP protein ( . coli) binds as a dimer to the two-fold symmetric operator sequence. The DNA is bent nearly 90deg in the complex. The turns are centered around two GT sequences (shown in black) of the recognition element.

See other pages where Capping proteins is mentioned: [Pg.546]    [Pg.414]    [Pg.415]    [Pg.415]    [Pg.23]    [Pg.26]    [Pg.44]    [Pg.45]    [Pg.51]    [Pg.53]    [Pg.89]    [Pg.540]    [Pg.104]    [Pg.359]    [Pg.497]    [Pg.61]    [Pg.89]    [Pg.311]    [Pg.153]    [Pg.224]    [Pg.227]    [Pg.17]    [Pg.20]    [Pg.20]    [Pg.21]    [Pg.21]    [Pg.22]    [Pg.719]    [Pg.728]    [Pg.19]   
See also in sourсe #XX -- [ Pg.44 ]




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