Colocalization of cortical microtubules and F-actin in Dipodascus magnusii using confocal laser scanning microscopy
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
12800500
DOI
10.1007/bf02930952
Knihovny.cz E-zdroje
- MeSH
- aktiny metabolismus MeSH
- buněčné dělení MeSH
- faloidin MeSH
- fluorescenční protilátková technika MeSH
- konfokální mikroskopie MeSH
- mikrotubuly ultrastruktura MeSH
- rhodaminy MeSH
- Saccharomycetales metabolismus ultrastruktura MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- aktiny MeSH
- faloidin MeSH
- rhodaminy MeSH
Distribution of microtubules and F-actin in aerobically growing cells of Dipodascus magnusii, belonging to the class Saccharomycetes was analyzed using immunofluorescence microscopy and labeling with rhodamine-tagged phalloidin. A conspicuous system of permanent cytoplasmic microtubules was observed in association with multiple nuclei. In elongating cells, helices of cytoplasmic microtubules appeared at the cell cortex. In cells approaching cytokinesis transversely oriented microtubules were revealed at incipient division sites. Confocal laser scanning microscopy showed a continuity of these transverse microtubules with the remaining microtubule network. The actin system of D. magnusii consisted of patches and filaments. Patches were found to accumulate at the tips of growing cells. Bands of fine actin filaments were usually observed before F-actin rings were established. A close cortical association of microtubules with the F-actin ring was documented on individual optical sections of labeled cells. Cells with developing septa showed medial F-actin discs associated at both sides with microtubules. Colocalization of cytoplasmic microtubules with actin filaments at the cortex of dividing cells supports a role of both cytoskeletal components in controlling cell wall growth and septum formation in D. magnusii.
Zobrazit více v PubMed
Microbiology (Reading). 1995 Jun;141 ( Pt 6):1289-1299 PubMed
Genes Dev. 1997 Nov 15;11(22):2939-51 PubMed
J Cell Biol. 1994 Apr;125(2):381-91 PubMed
Cell Motil Cytoskeleton. 1997;38(4):373-84 PubMed
J Cell Sci. 1989 Dec;94 ( Pt 4):647-56 PubMed
J Cell Biol. 1996 Mar;132(5):861-70 PubMed
Cell Biol Int Rep. 1991 Jul;15(7):607-10 PubMed
J Cell Sci. 1991 Aug;99 ( Pt 4):693-700 PubMed
J Cell Biol. 1984 Mar;98(3):847-58 PubMed
Methods Mol Biol. 1996;53:391-405 PubMed
Nature. 1992 Nov 5;360(6399):84-7 PubMed
FEBS Lett. 1974 Sep 1;45(1):263-6 PubMed
J Cell Sci. 2002 Sep 15;115(Pt 18):3575-86 PubMed
Biochim Biophys Acta. 1958 Feb;27(2):267-76 PubMed
Cytobiologie. 1978 Apr;16(3):393-411 PubMed
Eur J Cell Biol. 1988 Aug;46(3):499-505 PubMed
Biochim Biophys Acta. 1981 Apr 22;643(1):265-8 PubMed
Arch Microbiol. 1994;161(5):363-9 PubMed
J Cell Sci. 1984 Jul;69:47-65 PubMed
J Cell Sci. 1988 Mar;89 ( Pt 3):343-57 PubMed
Curr Opin Cell Biol. 1995 Feb;7(1):65-71 PubMed
Proc Natl Acad Sci U S A. 1996 Apr 30;93(9):3886-91 PubMed
Exp Cell Res. 2001 Jan 15;262(2):122-7 PubMed
Annu Rev Cell Biol. 1994;10:153-80 PubMed
Curr Genet. 2002 Apr;41(1):20-4 PubMed
Can J Microbiol. 1980 Feb;26(2):250-4 PubMed
Formaldehyde fixation is detrimental to actin cables in glucose-depleted S. cerevisiae cells
