Abstract
Plectin is a high molecular weight cytomatrix protein of widespread occurrence. In most cultured cell lines it was found to be part of cytoplasmic network arrays that appeared more dense and delicate than those of vimentin filaments after conventional fixation. Plectin and vimentin arrays appeared nearly identical, however, after extraction of cells with detergent, causing the release of a sizable fraction of cellular plectin (Herrmann and Wiche, 1983). These observations suggested that only part of the cytoplasmic plectin is associated with intermediate filaments while the rest is bound to more soluble structures or is forming a network of its own. There is, indeed, evidence that plectin interacts with several distinct cellular structures and that it acts as a general crosslinker of the cytomatrix (for review see Wiche, 1988). Here we report on molecular aspects of plectin’s interaction with vimentin.
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© 1989 Springer-Verlag Berlin Heidelberg
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Foisner, R., Feldman, B., Wiche, G. (1989). Plectin/Vimentin Interaction: Molecular Binding Domains and Regulation by Phosphorylation. In: Aebi, U., Engel, J. (eds) Cytoskeletal and Extracellular Proteins. Springer Series in Biophysics, vol 3. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-73925-5_32
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DOI: https://doi.org/10.1007/978-3-642-73925-5_32
Publisher Name: Springer, Berlin, Heidelberg
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