title: Plectin sidearms mediate interaction of intermediate filaments with microtubules and other components of the cytoskeleton.
abstract: By immunogold labeling, we demonstrate that "millipede-like" structures seen previously in mammalian cell cytoskeletons after removal of actin by treatment with gelsolin are composed of the cores of vimentin IFs with sidearms containing plectin. These plectin sidearms connect IFs to microtubules, the actin-based cytoskeleton and possibly membrane components. Plectin binding to microtubules was significantly increased in cells from transgenic mice lacking IFs and was reversed by microinjection of exogenous vimentin. These results suggest the existence of a pool of plectin which preferentially associates with IFs but may also be competed for by microtubules. The association of IFs with microtubules did not show a preference for Glu-tubulin. Nor did it depend upon the presence of MAP4 since plectin links were retained after specific immunodepletion of MAP4. The association of IFs with stress fibers survived actin depletion by gelsolin suggesting that myosin II minifilaments or components closely associated with them may play a role as plectin targets. Our results provide direct structural evidence for the hypothesis that plectin cross-links elements of the cytoskeleton thus leading to integration of the cytoplasm.
authors.affiliation: Laboratory of Molecular Biology, University of Wisconsin, Madison 53706, USA. tsvitkin@facstaff.wisc.edu
authors.forename: T M
authors.initials: TM
authors.lastname: Svitkina
authors.forename: A B
authors.initials: AB
authors.lastname: Verkhovsky
authors.forename: G G
authors.initials: GG
authors.lastname: Borisy
mesh_terms: D016475:3T3 Cells / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D000199:Actins / Q000378:metabolism; D000818:Animals; D001667:Binding, Competitive / Q000502:physiology; D002645:Chickens; D003593:Cytoplasm / Q000502:physiology; D003599:Cytoskeleton / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D004848:Epithelium / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D005347:Fibroblasts / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D005455:Fluorescent Antibody Technique; D018260:Gelsolin; D000882:Haplorhini; D006801:Humans; D007381:Intermediate Filament Proteins / Q000032:analysis / Q000502:physiology*; D007382:Intermediate Filaments / Q000737:chemistry / Q000378:metabolism*; D007425:Intracellular Membranes / Q000737:chemistry / Q000378:metabolism; D007668:Kidney / Q000166:cytology; D008297:Male; D051379:Mice; D008854:Microscopy, Electron; D008869:Microtubule-Associated Proteins / Q000378:metabolism; D008870:Microtubules / Q000737:chemistry / Q000378:metabolism*; D009218:Myosins / Q000378:metabolism; D051190:Plectin; D051381:Rats; D014746:Vimentin / Q000032:analysis / Q000502:physiology
chemical_list: D000199:Actins; D018260:Gelsolin; D007381:Intermediate Filament Proteins; D008869:Microtubule-Associated Proteins; C495332:PLEC protein, human; C495333:Plec protein, mouse; C495334:Plec protein, rat; D051190:Plectin; D014746:Vimentin; D009218:Myosins