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Pregled bibliografske jedinice broj: 124019

Dynamic organization of the actin system in the motile cells of Dictyostelium


Bretschneider, T.; Jonkman, J.; Köhler, J.; Medalia, O.; Barišić, Karmela; Weber, Igor; Stelzer, E.H.K.; Baumeister, W.; Gerisch, G.
Dynamic organization of the actin system in the motile cells of Dictyostelium // Journal of Muscle Research and Cell Motility, 23 (2002), 639-649 (međunarodna recenzija, članak, znanstveni)


Naslov
Dynamic organization of the actin system in the motile cells of Dictyostelium

Autori
Bretschneider, T. ; Jonkman, J. ; Köhler, J. ; Medalia, O. ; Barišić, Karmela ; Weber, Igor ; Stelzer, E.H.K. ; Baumeister, W. ; Gerisch, G.

Izvornik
Journal of Muscle Research and Cell Motility (0142-4319) 23 (2002); 639-649

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
Actin dynamics; Dictyostelium discoideum; FRAP

Sažetak
The actin system forms a supramolecular, membrane-associated network that serves multiple functions in Dictyostelium cells, including cell motility controlled by chemoattractant, phagocytosis, macropinocytosis, and cytokinesis. In executing these functions the monomeric G-actin polymerizes reversibly, and the actin .laments are assembled into membrane-anchored networks together with other proteins involved in shaping the networks and controlling their dynamics. Most impressive is the speed at which actin-based structures are built, reorganized, or disassembled. We used GFP-tagged coronin and Arp3, an intrinsic constituent of the Arp2/3 complex, as examples of proteins that are recruited to highly dynamic actin-.lament networks. By .uorescence recovery after photobleaching (FRAP), average exchange rates of cell-cortex bound coronin were estimated. A nominal value of 5 s for half-maximal incorporation of coronin into the cortex, and a value of 7 s for half-maximal dissociation from cortical binding sites has been obtained. Actin dynamics implies also .ow of F-actin from sites of polymerization to sites of depolymerization, i.e. to the tail of a migrating cell, the base of a phagocytic cup, and the cleavage furrow in a mitotic cell. To monitor this .ow, we expressed in Dictyostelium cells a GFP-tagged actinbinding fragment of talin. This fragment (GFP-TalC63) translocates from the front to the tail during cell migration and from the polar regions to the cleavage furrow during mitotic cell division. The intrinsic dynamics of the actin system can be manipulated in vivo by drugs or other probes that act either as inhibitors of actin polymerization or as stabilizers of .lamentous actin. In order to investigate structure– function relationships in the actin system, a technique of reliably arresting transient network structures is in demand. We discuss the potential of electron tomography of vitri.ed cells to visualize actin networks in their native association with membranes.

Izvorni jezik
Engleski

Znanstvena područja
Biologija, Farmacija



POVEZANOST RADA


Projekt / tema
0006631
0098073

Ustanove
Farmaceutsko-biokemijski fakultet, Zagreb,
Institut "Ruđer Bošković", Zagreb

Citiraj ovu publikaciju

Bretschneider, T.; Jonkman, J.; Köhler, J.; Medalia, O.; Barišić, Karmela; Weber, Igor; Stelzer, E.H.K.; Baumeister, W.; Gerisch, G.
Dynamic organization of the actin system in the motile cells of Dictyostelium // Journal of Muscle Research and Cell Motility, 23 (2002), 639-649 (međunarodna recenzija, članak, znanstveni)
Bretschneider, T., Jonkman, J., Köhler, J., Medalia, O., Barišić, K., Weber, I., Stelzer, E., Baumeister, W. & Gerisch, G. (2002) Dynamic organization of the actin system in the motile cells of Dictyostelium. Journal of Muscle Research and Cell Motility, 23, 639-649.
@article{article, year = {2002}, pages = {639-649}, keywords = {actin dynamics, Dictyostelium discoideum, FRAP}, journal = {Journal of Muscle Research and Cell Motility}, volume = {23}, issn = {0142-4319}, title = {Dynamic organization of the actin system in the motile cells of Dictyostelium}, keyword = {actin dynamics, Dictyostelium discoideum, FRAP} }

Časopis indeksira:


  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus
  • MEDLINE


Uključenost u ostale bibliografske baze podataka:


  • Chemical Abstracts
  • Excerpta Medica
  • Index Medicus