1999
Actin and Cytokinesis in Fission Yeasts
GABRIEL, Miroslav, Junpei ISHIGURO, Marie KOPECKÁ a Augustin SVOBODAZákladní údaje
Originální název
Actin and Cytokinesis in Fission Yeasts
Autoři
GABRIEL, Miroslav, Junpei ISHIGURO, Marie KOPECKÁ a Augustin SVOBODA
Vydání
Čs.Biol. spol. Brno, VII. Cytoskeletální klub, od s. 13-13, 1 s. VII. Cytoskeletální klub, 1999
Nakladatel
Čs. biologická společnost - Sekce biologie buňky
Další údaje
Jazyk
angličtina
Typ výsledku
Stať ve sborníku
Obor
10600 1.6 Biological sciences
Stát vydavatele
Česká republika
Utajení
není předmětem státního či obchodního tajemství
Kód RIV
RIV/00216224:14110/99:00003236
Organizační jednotka
Lékařská fakulta
Klíčová slova anglicky
actin; cytokinesis; fission yeasts
Štítky
Změněno: 28. 2. 2001 12:40, doc. MUDr. Miroslav Gabriel, CSc.
Anotace
V originále
F-actin occurs in several forms in yeasts:(i) hypothetically F-actin is a part of cytoskeletal subsystems of membrane cytoskeleton, (ii)microfilament cables are related to cell polarity, (iii) actin patches are at regions of surface growth, (iv) F-actin as a component of actin contractile ring realises cytokinesis. This report concentrates on the function of F-actin at cell division of fission yeasts. F-actin is essential, but not a single component of mechanism of cell division. Comparison of (i) actin mutant of S.pombe, incapable to aassemble actin cytoskeleton even at permissive temperature, and (ii) inhibition of actin polymerization by cytochalasin D in S.pombe and S. japonicus suggests that F-actin contractile ring is the main component ensuring the course of cytokinesis. While in actin mutant incapability of formation of actin cytoskeleton is followed by a complex of irreversible changes of cell functions and, consequently, also by incapability of cytokinesis, inhibition of F-actin polymerization enables to identify targets of consequences of incapability to polymerise new filament structures contractile ring including and to study reversibility of the processes blocked. Inhibition of actin polymerization by cytochalasins induces relatively reversible phenocopy modelling irreversible gene mutations.
Návaznosti
GA204/97/1150, projekt VaV |
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