title: Dynamics and segregation of cell-matrix adhesions in cultured fibroblasts.
abstract: Here we use time-lapse microscopy to analyse cell-matrix adhesions in cells expressing one of two different cytoskeletal proteins, paxillin or tensin, tagged with green fluorescent protein (GFP). Use of GFP-paxillin to analyse focal contacts and GFP-tensin to study fibrillar adhesions reveals that both types of major adhesion are highly dynamic. Small focal contacts often translocate, by extending centripetally and contracting peripherally, at a mean rate of 19 micrometers per hour. Fibrillar adhesions arise from the medial ends of stationary focal contacts, contain alpha5beta1 integrin and tensin but not other focal-contact components, and associate with fibronectin fibrils. Fibrillar adhesions translocate centripetally at a mean rate of 18 micrometers per hour in an actomyosin-dependent manner. We propose a dynamic model for the regulation of cell-matrix adhesions and for transitions between focal contacts and fibrillar adhesions, with the ability of the matrix to deform functioning as a mechanical switch.
authors.affiliation: Department of Molecular Cell Biology, The Weizmann Institute of Science, Rehovot 76100, Israel.
authors.forename: E
authors.initials: E
authors.lastname: Zamir
authors.forename: M
authors.initials: M
authors.lastname: Katz
authors.forename: Y
authors.initials: Y
authors.lastname: Posen
authors.forename: N
authors.initials: N
authors.lastname: Erez
authors.forename: K M
authors.initials: KM
authors.lastname: Yamada
authors.forename: B Z
authors.initials: BZ
authors.lastname: Katz
authors.forename: S
authors.initials: S
authors.lastname: Lin
authors.forename: D C
authors.initials: DC
authors.lastname: Lin
authors.forename: A
authors.initials: A
authors.lastname: Bershadsky
authors.forename: Z
authors.initials: Z
authors.lastname: Kam
authors.forename: B
authors.initials: B
authors.lastname: Geiger
mesh_terms: D000199:Actins / Q000378:metabolism; D000205:Actomyosin / Q000378:metabolism; D019086:Bridged Bicyclo Compounds, Heterocyclic / Q000494:pharmacology; D002448:Cell Adhesion / Q000502:physiology*; D002478:Cells, Cultured; D003598:Cytoskeletal Proteins / Q000235:genetics / Q000378:metabolism*; D003599:Cytoskeleton / Q000187:drug effects / Q000502:physiology*; D005109:Extracellular Matrix / Q000502:physiology*; D005347:Fibroblasts / Q000166:cytology; D017930:Genes, Reporter; D049452:Green Fluorescent Proteins; D006801:Humans; D007202:Indicators and Reagents / Q000378:metabolism; D008164:Luminescent Proteins / Q000235:genetics; D008840:Microfilament Proteins / Q000235:genetics / Q000378:metabolism*; D051419:Paxillin; D010750:Phosphoproteins / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D000070876:Tensins; D013844:Thiazoles / Q000494:pharmacology; D053778:Thiazolidines; D014162:Transfection
chemical_list: D000199:Actins; D019086:Bridged Bicyclo Compounds, Heterocyclic; D003598:Cytoskeletal Proteins; D007202:Indicators and Reagents; D008164:Luminescent Proteins; D008840:Microfilament Proteins; C496061:PXN protein, human; D051419:Paxillin; D010750:Phosphoproteins; D011994:Recombinant Proteins; D000070876:Tensins; D013844:Thiazoles; D053778:Thiazolidines; D049452:Green Fluorescent Proteins; D000205:Actomyosin; C037067:latrunculin A