Cytoskeleton proteins

Italiano, J. E., Jr., Stewart, M., and Roberts, T. M. (1999). Localized depolymerization of the major sperm protein cytoskeleton correlates with the forward movement of the cell body in the amoeboid movement of nematode sperm. J. Cell Biol. 146, 1087-1095. 

Polymerized lipids do not occur in natural cell membranes. Nature tends to support fragile membrane structures with polymeric skeletons, i.e. protein cytoskeletons, polysaccharide cell walls etc. Analogous synthetic polymeric nets are simply constructed from polymerizable counterions. Negatively charged dihexadecyl phosphate vesicles can be neutralized with choline methacrylate polymerization of the latter produces a polycationic vesicle coat which is not inserted into the membrane (Figure 4.30). A cytoskeleton at the... 

Volume 43 Membrane Protein-Cytoskeleton Interactions (1996) Edited by W. James Nelson... 

The modem era of biochemistry and molecular biology has been shaped not least by the isolation and characterization of individual molecules. Recently, however, more and more polyfunctional macromolecular complexes are being discovered, including nonrandomly codistributed membrane-bound proteins [41], These are made up of several individual proteins, which can assemble spontaneously, possibly in the presence of a lipid membrane or an element of the cytoskeleton [42] which are themselves supramolecular complexes. Some of these complexes, e.g. snail haemocyanin [4o], are merely assembled from a very large number of identical subunits vimses are much larger and more elaborate and we are still some way from understanding the processes controlling the assembly of the wonderfully intricate and beautiful stmctures responsible for the iridescent colours of butterflies and moths [44]. 

Fig. 1. The GP Ib-IX-V complex. The complex consists of seven transmembrane polypeptides denoted GP Iba (mol wt 145,000), GP IbP (mol wt 24,000), GPIX (mol wt 17,000) and GP V (mol wt 82,000), in a stoichiometry of 2 2 2 1. The hatched region represents the plasma membrane. The area above the hatched region represents the extracellular space that below represents the cytoplasm. The complex is a major attachment site between the plasma membrane and the cytoskeleton. Two molecules associated with the cytoplasmic domain are depicted a 14-3-3 dimer, which may mediate intracellular signaling, and actin-binding protein, which connects the complex to the cortical cytoskeleton and fixes its position and influences its function.

Just how fast can proteins move in a biological membrane Many membrane proteins can move laterally across a membrane at a rate of a few microns per minute. On the other hand, some integral membrane proteins are much more restricted in their lateral movement, with diffusion rates of about 10 nm/sec or even slower. These latter proteins are often found to be anchored to the cytoskeleton (Chapter 17), a complex latticelike structure that maintains the cell s shape and assists in the controlled movement of various substances through the ceil. 

C. botulinum C3-toxin and related toxins Rho proteins ADP-ribosylation Inhibition of RhoA, B,C Destruction of the cytoskeleton... 

Catenins are defined as cytoplasmic interaction partners of cadherins that form a chain of proteins ( catena, latin for chain), which connects cadherins to the actin cytoskeleton. 

Interactions with the cytoskeleton seem to be responsible for the processing and the targeting of the Na+/fC+-ATPase to the appropriate compartment structures. Protein kinases are considered to play an essential role in modulation of the sodium pump. 

The cytoskeleton also contains different accessory proteins, which, in accordance with their affinities and functions, are designated as microtubule-associated proteins (MAPs), actin-binding proteins (ABPs), intermediate-filament-associated proteins (IFAPs), and myosin-binding proteins. This chapter is focused on those parts of the cytoskeleton that are composed of microfilaments and microtubules and their associated proteins. The subject of intermediate filaments is dealt with in detail in Volume 2. 

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 ... 

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 ... 

The membrane cytoskeleton (inclusive of the submembranous actin-spec-trin network) may function in the establishment and maintenance of restricted domains of specific proteins on the plasma membrane of polarized epithelial cells (Rodriguez-Boulan and Nelson, 1989 Mays et al., 1994). 

A family of transmembrane proteins referred to as integrins is capable of interactions with extracellular ligands as well as with the cytoskeleton. These have been implicated in cell-to-cell interactions through the extracel-... 

It is of interest that proteins termed motility factors (55-70 kD) are secreted by fetal cells and some tumor cells. These proteins act as autocrine factors and stimulate rapid movement by these cells. Motility factors induce the formation of cell processes that are packed with actin filaments and have an increased number of receptors for the matrix proteins laminin and fibronectin. The latter enhance the ability of the cells to bind to the extracellular matrix. Thus, it is likely that motility factors influence the organization of the cytoskeleton through changes taking place at the cell surface (reviewed by Warn and Dowrick, 1989). 

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

Mays, R.W., Beck, K.A.. Nelson, W.J. (1994). Organization and function of the cytoskeleton in polarized epithelial cells a component of the protein sorting machinery. Curr. Opin. Cell Biol. 6, 16-24. 

The Role of Myosins in Cell Locomotion The Role of Actin-Binding Proteins in Cell Locomotion The Transduction of Extracellular Motility Signals to the Cytoskeleton Lipid Flow and Cell Locomotion The Role of Cell Locomotion in Metastasis Intracellular Motility Microtubule-Based Intracellular Motility... 

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