Abstract

This chapter presents studies on the mechanism by which one subcellular structure, cytoplasmic microtubule (MT) may interact with membranes to regulate surface topography. The degree of MT assembly and MT–membrane interaction in intact cells varies in a dynamic manner, depending on binding events occurring at the surface. The degree of assembly of MT and extent of MT–membrane interactions appears to be enhanced after ligand or particle binding with surface receptors. This enhancement may be mediated in part via the stimulation of cyclic GMP generation, which seems to increase MT stability. The mobility of proteins in cell membranes is regulated at least in part by MT. An intermediate step, the generation of cyclic GMP may follow ligand or particle binding and determine the stability of MT and/or of MT–membrane interaction. The immobilization of leukocyte membranes by phenylglyoxal is unrelated to changes in lipid fluidity. An arginine-rich intramembranous protein (or proteins) is involved in determining the mobility of proteins in leukocyte membranes and in controlling the deformability of the whole membrane. Although proteins are mobile in cell membranes, it is clear that they do not always diffuse at random in the lipid matrix of the membrane but rather are subject to considerable restraints on mobility.

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