Cell membranes interaction with cytoskeleton

Fowler XE. and Quantrano R.S. 1997. Plant cell morphogenesis plasma membrane interactions with the cytoskeleton and cell wall. Annu Rev Cell Dev Biol 13 697-743. 

Figure 10.7 The EGF receptor. The N-terminal, extracellular region of the receptor contains 622 amino acids. It displays two cysteine-rich regions, between which the ligand-binding domain is located. A 23 amino acid hydrophobic domain spans the plasma membrane. The receptor cytoplasmic region contains some 542 amino acids. It displays a tyrosine kinase domain, which includes several tyrosine autophosphorylation sites, and an actin-binding domain that may facilitate interaction with the cell cytoskeleton...

Mechanical functions of cells require interactions between integral membrane proteins and the cytoskeleton 29 The spectrin-ankyrin network comprises a general form of membrane-organizing cytoskeleton within which a variety of membrane-cytoskeletal specializations are interspersed 29 Interaction of rafts with cytoskeleton is suggested by the results of video microscopy 29... 

Several ILC studies covering drug interaction with liposomes and, correspondingly, proteoliposomes, cytoskeleton-depleted red blood cell membrane vesicles, red blood cell membranes, or red cells and ghosts have been reported (7,8,21-28,40,76,91,92,94). The log Ks values for interaction of... 

A characteristic feature of the SuSy isoforms is a conserved phosphorylated serine residue near the N-terminus [8-10]. In-vivo studies have demonstrated that phosphorylation and dephosphorylation direct the distribution of SuSy isoforms in the plant cell [10-12]. The soluble phosphorylated SuSy interacts with the actin cytoskeleton in the cytoplasm [13], and the dephosphorylated SuSy isoforms are targeted to the cell membrane to form complexes with other enzymes, e.g., glucan synthase, catalyzing cellulose biosynthesis from sucrose [4, 10, 14]. In this respect, recent studies on the dephosphorylated enzymes by cloning and expression of SMS genes in E. coli have shown differences in some biochemical features when compared to the enzymes isolated from the corresponding plant material. Recom-... 

This process is an early morphological change in cells often seen in isolated cells in vitro but also known to occur in vivo. The blebs, which appear before membrane permeability alters, are initially reversible. However, if the toxic insult is sufficiently severe and the cellular changes become irreversible, the blebs may rupture. If this occurs, vital cellular components may be lost and cell death follows. The occurrence of blebs may be due to damage to the cytoskeleton, which is attached to the plasma membrane as described above. The cause may be an increase in cytosolic Ca2+, interaction with cytoskeletal proteins, or modification of thiol groups (see below). 

What is the function of the membrane skeleton There is a group of hereditary diseases including spherocytosis in which erythrocytes do not maintain their biconcave disc shape but become spherical or have other abnormal shapes and are extremely fragile.269 272 Causes of spherocytosis include defective formation of spectrin tetramers and defective association of spectrin with ankyrin or the band 4.1 protein.265 273 Thus, the principal functions of these proteins in erythrocytes may be to strengthen the membrane and to preserve the characteristic shape of erythrocytes during their 120-day lifetime in the bloodstream. In other cells the spectrins are able to interact with microtubules, which are absent from erythrocytes, and to microtubule-associated proteins of the cytoskeleton (Chapter 7, Section F).270 In nerve terminals a protein similar to erythrocyte protein 4.1 may be involved in transmitter release.274 The cytoskeleton is also actively involved in transmembrane signaling. 

The linear polypeptide chains of a protein fold in a highly specific way that is determined by the sequence of amino acids in the chains. Many proteins are composed of two or more polypeptides. Certain proteins function in structural roles. Some structural proteins interact with lipids in membrane structures. Others aggregate to form part of the cytoskeleton that helps to give the cell its shape. Still others are the chief components of muscle or connective tissue. Enzymes constitute yet another major class of proteins, which function as catalysts that accelerate and direct biochemical reactions. 

The contacts between two adjoining cell membranes are stabilized by specific cell adhesion molecules (CAMs), which include the Ca+2-dependent cadherins. These molecules appear to lead the way for cell-cell communications and are involved in mechanochemical transduction via cell-cell interactions. In some cell types, cadherins are concentrated within adherens junctions that are stretch-sensitive and their extracellular domains interact with cadherins on adjacent cells whereas their cytoplasmic domains provide attachment to the actin cytoskeleton via catenins and other cytoskeletal proteins. The Rho family is required for the establishment and maintenance of cadherin-based adherens junctions. The type of cadherin expressed in a cell can affect the specificity and the physiological properties of cell-cell interactions. 

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