title: Microtubules and actin filaments are not critically involved in the biogenesis of epithelial cell surface polarity.
abstract: We have studied the role of microtubules and actin filaments in the biogenesis of epithelial cell surface polarity, using influenza hemagglutinin and vesicular stomatitis G protein as model apical and basolateral proteins in infected Madin-Darby canine kidney cells. Addition of colchicine or nocodazole to confluent monolayers at concentrations sufficient to completely disassemble microtubules did not affect the asymmetric budding of influenza or vesicular stomatitis virus and only slightly reduced the typical asymmetric surface distribution of their envelope proteins, despite extensive cytoplasmic redistribution of the Golgi apparatus. Alteration of microtubular function by taxol or dissociation of actin filaments by cytochalasin D also failed to have a significant effect. Furthermore, neither colchicine nor cytochalasin D pretreatment blocked the ability of subconfluent Madin-Darby canine kidney cells to sustain polarized budding of influenza virus a few hours after attachment to the substrate. Our results indicate that domain-specific microtubule or actin filament "tracks" are not responsible for the vectorial delivery of apically or basolaterally directed transport vesicles. In conjunction with currently available evidence, they are compatible with a model in which receptors in the cytoplasmic aspect of apical or basolateral regions provide vectoriality to the transport of vesicles carrying plasma membrane proteins to their final surface localization.
authors.forename: P J
authors.initials: PJ
authors.lastname: Salas
authors.forename: D E
authors.initials: DE
authors.lastname: Misek
authors.forename: D E
authors.initials: DE
authors.lastname: Vega-Salas
authors.forename: D
authors.initials: D
authors.lastname: Gundersen
authors.forename: M
authors.initials: M
authors.lastname: Cereijido
authors.forename: E
authors.initials: E
authors.lastname: Rodriguez-Boulan
mesh_terms: D008841:Actin Cytoskeleton / Q000502:physiology*; D000199:Actins / Q000502:physiology; D000470:Alkaloids / Q000494:pharmacology; D000818:Animals; D001562:Benzimidazoles / Q000494:pharmacology; D002451:Cell Compartmentation / Q000187:drug effects; D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism; D003078:Colchicine / Q000494:pharmacology; D015638:Cytochalasin D; D003572:Cytochalasins / Q000494:pharmacology; D003599:Cytoskeleton / Q000502:physiology*; D004285:Dogs; D004848:Epithelium / Q000648:ultrastructure*; D005089:Exocytosis; D006389:Hemagglutinins, Viral / Q000378:metabolism; D007668:Kidney / Q000166:cytology; D008562:Membrane Glycoproteins; D008565:Membrane Proteins / Q000378:metabolism; D008854:Microscopy, Electron; D008870:Microtubules / Q000502:physiology*; D015739:Nocodazole; D009975:Orthomyxoviridae; D017239:Paclitaxel; D014404:Tubulin / Q000502:physiology; D014721:Vesicular stomatitis Indiana virus; D014759:Viral Envelope Proteins; D014764:Viral Proteins / Q000378:metabolism; D014779:Virus Replication
chemical_list: D000199:Actins; D000470:Alkaloids; D001562:Benzimidazoles; D003572:Cytochalasins; C028391:G protein, vesicular stomatitis virus; D006389:Hemagglutinins, Viral; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D014404:Tubulin; D014759:Viral Envelope Proteins; D014764:Viral Proteins; D015638:Cytochalasin D; D017239:Paclitaxel; D015739:Nocodazole; D003078:Colchicine