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Plectin and IFAP-300K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin.

Structural and functional characteristics of plectin from intermediate filament preparations of rat glioma C6 cells were compared to those of the intermediate filament-associated protein of Mr = 300,000 (IFAP-300K) of baby hamster kidney cells (Yang, H.-S., Lieska, N., Goldman, A.E., and Goldman, R.D. (1985) J. Cell Biol. 100, 620-631). After radiolabeling and proteolytic digestion under varied conditions, both proteins yielded nearly identical peptide maps. Immunological cross-reactivity, co-migration on one- and two-dimensional high-resolution gels, chromatofocusing, and amino acid analysis demonstrated structural homology as well. In vivo labeling with 32Pi showed that plectin was the target for cAMP-independent protein kinases which phosphorylated 18-kDa domains at the end(s) of the molecule. Previously reported phosphorylation sites for cAMP-dependent and a newly identified site for Ca2+/calmodulin-dependent protein kinases were located on different domains. In solid-phase binding assays, plectin bound to vimentin, microtubule-associated proteins 1 and 2, the 240-kDa chain of brain fodrin, and alpha-spectrin from human erythrocytes. Similar characteristics were revealed for corresponding 300-kDa components of various other cell lines, supporting the concept that plectin is a general cytoskeletal cross-linking element, probably of multiple function.

Pubmed ID: 3027087


  • Herrmann H
  • Wiche G


The Journal of biological chemistry

Publication Data

January 25, 1987

Associated Grants


Mesh Terms

  • Animals
  • Carrier Proteins
  • Cell Line
  • Chemistry, Physical
  • Cricetinae
  • Cyclic AMP
  • Glioma
  • Humans
  • Intermediate Filament Proteins
  • Kidney
  • Microfilament Proteins
  • Microtubule-Associated Proteins
  • Molecular Weight
  • Phosphorylation
  • Physicochemical Phenomena
  • Plectin
  • Protein Kinases
  • Proteins
  • Rats
  • Spectrin