Intermediate filament protein

Figure 14.5 The domain organization of intermediate filament protein monomers. Most intermediate filament proteins share a similar rod domain that is usually about 310 amino acids long and forms an extended a helix. The amino-terminal and carboxy-terminal domains are non-a-helical and vary greatly in size and sequence in different intermediate filaments.

The leucine zipper DNA-binding proteins, described in Chapter 10, are examples of globular proteins that use coiled coils to form both homo- and heterodimers. A variety of fibrous proteins also have heptad repeats in their sequences and use coiled coils to form oligomers, mainly dimers and trimers. Among these are myosin, fibrinogen, actin cross-linking proteins such as spectrin and dystrophin as well as the intermediate filament proteins keratin, vimentin, desmin, and neurofilament proteins. 

The major types of cytoskeletal filaments are 7-nm-thick microfilaments. 25-nm-thick microtubules, and 10-nm-thick intermediate filaments (IPs). These are respectively composed of actin, tubulin, and a variety of interrelated sparsely soluble fibrous proteins termed intermediate filament proteins. In addition, thick myosin filaments are present in large numbers in skeletal and heart muscle cells and in small numbers in many other types of eukaryotic cells. 

Dent, J. A., Poison, A. G., and Klymkowsky, M. W. (1989) A whole-mount immnnocytochemical analysis of the expression of the intermediate filament protein vimentin in Xenopns. Develop. 105, 61-74. 

Carnosine can affect gene expression. Ikeda et al. (1999) showed that carnosine markedly upregulates vimentin synthesis in cultured rat fibroblasts, while an association between carnosine and vimentin, a cytoskele-tal, intermediate filament protein has been noted in glial cells and neurons (Bonfanti et al., 1999). Interestingly, it has also been shown that the protease, oxidized protein hydrolase (OPH), is coexpressed with vimentin in COS cells (Shimizu et al., 2004). Thus, it is at least possible that carnosine could induce synthesis of OPH in the cultured human fibroblasts and thereby increase the cellular ability to eliminate oxidized... 

Lendahl, U., Zimmerman, L.B., McKay, R.D. (1990). CNS stem cells express a new class of intermediate filament protein. Cell, 60, 585-95. 

The two-stranded a-helical coiled coil is now recognized as one of natures favorite ways of creating a dimerization motif and has been predicted to occur in a diverse group of over 200 proteins.111 This structure consists of two amphipathic, right-handed a-helices that adopt a left-handed supercoil, analogous to a two-stranded rope where the nonpolar face of each a-helix is continually adjacent to that of the other helix. 2 This structure was first postulated by Crick to explain the X-ray diffraction pattern of a-keratin in the absence of sequence information.Pl The coiled-coil dimerization motif is natures way of creating a rod-like molecule that perhaps plays only a structural role in many fibrous proteins, such as the kmef (keratin, myosin, epidermis, fibrinogen) class 3,4 and the intermediate filament proteins)5 6 ... 

McLachlan, A. D., and Stewart, M. (1982). Periodic charge distribution in the intermediate filament proteins desmin and vimentin./. Mol. Biol. 162, 693-698. 

Steinert, P. M., Chou, Y.-H., Prahlad, V., Parry, D. A. D., Marekov, L. N., Wu, K. C., Jang, S.-I., and Goldman, R. D. (1999b). A high molecular weight intermediate filament-associated protein in BHK-21 cells is nestin, a Type VI intermediate filament protein Limited co-assembly in vitro to form heteropolymers with Type III vimen-tin and Type IV a-Internexin./ Biol. Chem. 274, 9881-9890. 

Fisher, D. Z., Chaudhary, N., and Blobel, G. (1986). cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins. Proc. Natl. Acad. Sci. USA 83, 6450-6454. 

Herrling, J., and Sparrow, L. G. (1991). Interactions of intermediate filament proteins from wool. Int. J. Biol. Macromol. 13, 115-119. 

Herrmann, H., Haner, M., Brettel, M., Ku, N-O., and Aebi, U. (1999). Characterization of distinct early assembly units of different intermediate filament proteins. J. Mol. Biol. 286, 1403-1420. 

McKeon, F. D., Kirschner, M. W., and Caput, D. (1986). Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins. Nature (London) 319, 463-468. 

Parry, D. A. D., Conway, J. F., and Steinert, P. M. (1986). Structural studies on lamin Similarities and differences between lamin and intermediate-filament proteins. Biochem. J. 238, 305—308. 

Quinlan, R., Hutchison, C., and Lane, B. (1994). Intermediate filament proteins. Protein Profile 1, 779-911. 

Smith, T. A., Hempstead, P. D., Palliser, C. C., and Parry, D. A. D. (2003). Modeling o-helical coiled-coil interactions The axial and azimuthal alignment of IB segments from vimentin intermediate filaments. Proteins 50, 207-212. 

Beilin, R. M., Sernett, S. W., Becker, B., Ip, W., Huiatt, T. W., and Robson, R. M. (1999). Molecular characteristics and interactions of the intermediate filament protein synemin. Interactions with alpha-actinin may anchor synemin-containing heterofilaments./. Biol. Chem. 274, 29493-29499. 

Craig, S. W., and Pardo, J. V. (1983). Gamma actin, spectrin, and intermediate filament proteins colocalize with vinculin at costameres, myofibril-to-sarcolemma attachment sites. Cell Motil. 3, 449-462. 

Foisner, R., Bohn, W., Mannweiler, K., and Wiche, G. (1995). Distribution and ultrastructure of plectin arrays in subclones of rat glioma C6 cells differing in intermediate filament protein (vimentin) expression./. Struct. Biol. 115, 304—317. 

Foisner, R., Leichtfried, F. E., Herrmann, H., Small, J. V., Lawson, D., and Wiche, G. (1988). Cytoskeleton-associated plectin in situ localization, in vitro reconstitution, and binding to immobilized intermediate filament proteins. /. Biol. Chem. 106, 723-733. 

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