Actin Regulation

Hatanaka, H., K. Ogura, K. Moriyama, S. Ichikawa, I. Yahara, and F. Inagaki. 1996. Tertiary structure of destrin and structural similarity between two actin-regulating protein families. Cell. 85 1047-55. [Pg.66]

Rho proteins are involved in regulation of the actin cytoskeleton and induce formation of stress fibers and focal adhesions (Paterson et al., 1990 Ridley and Hall, 1992 Tominaga et al., 1993 Laudanna et al., 1996). Most probably independently of their role in actin regulation, Rho proteins have been proposed to participate as molecular switches in the control of phosphoinositide-3-kinase (Zhang et al., 1993), phosphatidylinositol-4-phosphate-5-kinase (Chong et al.. [Pg.64]

Frame, M.G. and Brunton, V.G. (2002). Advances in Rho-dependent actin regulation and oncogenic transformation. Cum Opin. Genet. Dev. 12, 36-43. [Pg.297]

Ketelaar T, Faivre-Moskalenko C., Esseling J.J., de Ruijter N.C.A., Grierson C.S., Dogterom M., and Emons A.M.C. 2002. Positioning of nuclei in Arabidopsis root hairs an actin-regulated process of tip growth. The Plant Cell 14 2941-2955. [Pg.196]

In addition to the major proteins of striated muscle (myosin, actin, tropomyosin, and the troponins), numerous other proteins play important roles in the maintenance of muscle structure and the regulation of muscle contraction. Myosin and actin together account for 65% of the total muscle protein, and tropomyosin and the troponins each contribute an additional 5% (Table 17.1). The other regulatory and structural proteins thus comprise approximately 25% of the myofibrillar protein. The regulatory proteins can be classified as either myosin-associated proteins or actin-associated proteins. [Pg.546]

By binding to F-actin, actin binding proteins (ABPs) stabilize F-actin or regulate its turnover. Known ABPs are proteins such as a-actinin, talin, tensin, filamin, nexilin, fimbrin, and vinculin. [Pg.13]

In Drosophila, Fat functions as a tumor suppressor gene and dachsous is involved in thorax, leg, and wing development. Several human and mouse homologs have been identified. FAT1 regulates actin filaments, and the Fail knockout leads to defects in glomerular slit formation [3]. [Pg.308]

Stimulation of PKA and PKC inhibit NHE5 activity, as does hyperosmolarity, resembling the responsiveness of NHE3. NHE5 may also be regulated by the actin cytoskeleton, but further work is required to validate this notion and clarify the exact mechanism. [Pg.811]

The major relaxing transmitters are those that elevate the cAMP or cGMP concentration (Fig. 3). Adenosine stimulates the activity of cAMP kinase. The next step is not clear, but evidence has been accumulated that cAMP kinase decreases the calcium sensitivity of the contractile machinery. In vitro, cAMP kinase phosphorylated MLCK and decreased thereby the affinity of MLCK for calcium-calmodulin. However, this regulation does not occur in intact smooth muscle. Possible other substrate candidates for cAMP kinase are the heat stable protein HSP 20, (A heat stable protein of 20 kDa that is phosphorylated by cGMP kinase. It has been postulated that phospho-HSP 20 interferes with the interaction between actin and myosin allowing thereby smooth muscle relaxation without dephosphorylation of the rMLC.) Rho A and MLCP that are phosphorylated also by cGMP kinase I (Fig. 3). [Pg.1144]

SARA is a scaffolding protein that regulates the subcellular localization of inactivated R-Smads, potentially scaffolding the TGF-P receptor kinase to the Smad 2 substrate. Filamins are a family of actin polymerization proteins that also form scaffolds for a range of signaling proteins including SAP kinases such as MKK-4, small GTPases Rho and Ras, as well as Smad 2 and Smad 5. [Pg.1230]

More than 50 proteins have been discovered in the cytosol of nonmuscle cells that bind to actin and affect the assembly and disassembly of actin filaments or the cross-linking of actin filaments with each other, with other filamentous components of the cytoskeleton, or with the plasma membrane. Collectively, these are known as actin-binding proteins (ABPs). Their mechanisms of actions are complex and are subject to regulation by specific binding affinities to actin and other molecules, cooperation or competition with other ABPs, local changes in the concentrations of ions in the cytosol, and physical forces (Way and Weeds, 1990). Classifications of ABPs have been proposed that are based on their site of binding to actin and on their molecular structure and function (Pollard and Cooper, 1986 Herrmann, 1989 Pollard et al., 1994). These include the following ... [Pg.22]

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]

Thus far, microtubules and actin filaments and their associated proteins have been discussed to advantage as independent cytoskeletal components. In actual fact, all of the components of the cytoskeleton (including intermediate filaments) are precisely integrated with one another (Langford, 1995), as well as with various cytoplasmic organelles, the nuclear membrane, the plasma membrane, and the extracellular matrix. In its totality the cytoskeleton subserves many coordinated and regulated functions in the cell ... [Pg.34]

Hall, A. (1994). Small GTP-binding proteins and the regulation of the actin cytoskeleton. Ann. Rev. Cell Biol. 10,31-54. [Pg.38]

Tilney, L.G., Bonder, E.M., Coluccio, L.M., Moosekar, M.S. (1983). Actin from Thyone sperm assembles on only one end of an actin filament A behavior regulated by profilin. J. Cell Biol. 97, 112-124. [Pg.41]

Actin Polymerization Regulation by Divalent Metal Ion and Nucleotide Bindings ATP Hydrolysis and Actin Binding Proteins... [Pg.43]

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