ARP2 and ARP3 are localized to sites of actin filament nucleation in tobacco BY-2 cells
Jazyk angličtina Země Rakousko Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
- MeSH
- bicyklické sloučeniny heterocyklické farmakologie MeSH
- buněčné jádro metabolismus MeSH
- imunoblotting MeSH
- mikrofilamenta metabolismus MeSH
- protein 2 související s aktinem metabolismus MeSH
- protein 3 související s aktinem metabolismus MeSH
- tabák cytologie účinky léků metabolismus MeSH
- thiazolidiny MeSH
- thiazoly farmakologie MeSH
- transport proteinů MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- bicyklické sloučeniny heterocyklické MeSH
- latrunculin B MeSH Prohlížeč
- protein 2 související s aktinem MeSH
- protein 3 související s aktinem MeSH
- thiazolidiny MeSH
- thiazoly MeSH
Complete depolymerization of actin filaments (AFs) at low temperature (0 degrees C) is followed by the formation of transient actin structures at 25 degrees C in tobacco BY-2 cells (Nicotiana tabacum L.). Using antibodies against fission yeast actin-related proteins (ARP2 and ARP3), we show here that transient actin structures (dots, dotted filaments, rods) colocalize with epitopes stained by these antibodies and thus are likely to represent sites of actin filament nucleation (SANs). In contrast to the cold-induced disassembly of AFs, no transient actin structures were detectable during recovery of AFs from latrunculin B-induced depolymerization. However, the staining pattern obtained with ARP antibodies in latrunculin B-treated cells was similar to that in controls and cold-treated cells. This suggests that, in addition to the complete depolymerization of AFs, disruption of other cellular structures is needed for the formation of transient actin structures during the early phase of recovery from cold treatment.
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Proc Natl Acad Sci U S A. 1998 May 26;95(11):6181-6 PubMed
Development. 1999 Dec;126(24):5559-68 PubMed
Plant Physiol. 1998 Nov;118(3):917-28 PubMed
Plant Physiol. 1997 Nov;115(3):875-879 PubMed
Cell. 1999 Apr 16;97(2):221-31 PubMed
Plant Physiol. 1991 Sep;97(1):175-81 PubMed
Protoplasma. 2003 Sep;222(1-2):45-52 PubMed
Curr Biol. 2004 Jan 6;14(1):1-10 PubMed
J Cell Biol. 2002 Aug 19;158(4):669-79 PubMed
Plant Cell Physiol. 2004 Jul;45(7):813-22 PubMed
Plant Physiol. 1991 Sep;97(1):182-7 PubMed
Annu Rev Cell Dev Biol. 2002;18:247-88 PubMed
Traffic. 2004 Nov;5(11):838-46 PubMed
Curr Biol. 2003 Aug 5;13(15):1341-7 PubMed
Curr Opin Plant Biol. 2002 Dec;5(6):502-6 PubMed
Nat Cell Biol. 2000 Jun;2(6):376-8 PubMed
Curr Opin Plant Biol. 2003 Dec;6(6):561-7 PubMed
Plant Physiol. 2003 Aug;132(4):2034-44 PubMed
Curr Biol. 1999 Apr 22;9(8):405-15 PubMed
Plant Physiol. 1990 May;93(1):83-8 PubMed
FEBS Lett. 2004 May 21;566(1-3):281-6 PubMed
Nature. 2000 Apr 27;404(6781):1007-11 PubMed
Plant Cell Physiol. 2003 Jul;44(7):676-86 PubMed
J Cell Biol. 1997 Jul 28;138(2):375-84 PubMed
Stain Technol. 1972 Jul;47(4):189-94 PubMed
Plant Cell. 2003 Jul;15(7):1632-45 PubMed
J Cell Biol. 2003 Feb 3;160(3):409-21 PubMed
Mol Biol Cell. 2002 Feb;13(2):621-31 PubMed
J Cell Biol. 1996 Jul;134(1):117-32 PubMed
Development. 2004 Sep;131(17):4345-55 PubMed
Science. 2001 Nov 23;294(5547):1679-84 PubMed
J Cell Biol. 1999 May 31;145(5):1009-26 PubMed
Plant Cell. 2004 Sep;16(9):2335-49 PubMed
Mol Biol Cell. 2002 Mar;13(3):866-79 PubMed
Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15362-7 PubMed
EMBO J. 1996 Dec 2;15(23):6438-46 PubMed
Curr Biol. 2004 Aug 10;14(15):1410-4 PubMed
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