Tools for visualization of phosphoinositides in the cell nucleus
Jazyk angličtina Země Německo Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
26847181
DOI
10.1007/s00418-016-1409-8
PII: 10.1007/s00418-016-1409-8
Knihovny.cz E-zdroje
- Klíčová slova
- Nucleus, PI(4)P, PI(4,5)P2, Phosphoinositides,
- MeSH
- buněčné jadérko chemie metabolismus MeSH
- fluorescenční mikroskopie MeSH
- fluorescenční protilátková technika nepřímá MeSH
- fosfatidylinositoly analýza imunologie metabolismus MeSH
- konfokální mikroskopie MeSH
- kultivované buňky MeSH
- lidé MeSH
- protilátky imunologie MeSH
- reakce antigenu s protilátkou MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- fosfatidylinositoly MeSH
- protilátky MeSH
Phosphoinositides (PIs) are glycerol-based phospholipids containing hydrophilic inositol ring. The inositol ring is mono-, bis-, or tris-phosphorylated yielding seven PIs members. Ample evidence shows that PIs localize both to the cytoplasm and to the nucleus. However, tools for direct visualization of nuclear PIs are limited and many studies thus employ indirect approaches, such as staining of their metabolic enzymes. Since localization and mobility of PIs differ from their metabolic enzymes, these approaches may result in incomplete data. In this paper, we tested commercially available PIs antibodies by light microscopy on fixed cells, tested their specificity using protein-lipid overlay assay and blocking assay, and compared their staining patterns. Additionally, we prepared recombinant PIs-binding domains and tested them on both fixed and live cells by light microscopy. The results provide a useful overview of usability of the tools tested and stress that the selection of adequate tools is critical. Knowing the localization of individual PIs in various functional compartments should enable us to better understand the roles of PIs in the cell nucleus.
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J Struct Biol. 2015 Dec;192(3):342-8 PubMed
Science. 2001 Jun 15;292(5524):2041-50 PubMed
Cell. 1998 Nov 25;95(5):625-36 PubMed
J Biol Chem. 1983 Aug 10;258(15):9360-7 PubMed
J Biol Chem. 2006 Jun 16;281(24):16740-9 PubMed
Mol Biol Cell. 2008 Feb;19(2):711-21 PubMed
Crit Rev Biochem Mol Biol. 2011 Oct;46(5):436-57 PubMed
Curr Biol. 1999 Apr 22;9(8):433-6 PubMed
J Physiol. 2008 Jun 15;586(12):2855-71 PubMed
Biochim Biophys Acta. 2003 Feb 20;1631(1):61-71 PubMed
Nature. 2008 Feb 21;451(7181):1013-7 PubMed
BMC Cell Biol. 2009 Sep 21;10:67 PubMed
Exp Cell Res. 2008 Aug 1;314(13):2376-88 PubMed
Biochem J. 2009 Jul 29;422(1):23-35 PubMed
Mol Cell. 2006 Sep 1;23(5):685-95 PubMed
Biochem J. 1999 Dec 15;344 Pt 3:929-36 PubMed
Nucleus. 2013 Nov-Dec;4(6):478-86 PubMed
J Biol Chem. 1994 Mar 18;269(11):7847-50 PubMed
EMBO J. 2000 Sep 1;19(17):4577-88 PubMed
J Biol Chem. 1998 Nov 13;273(46):30497-508 PubMed
J Cell Sci. 2001 Jul;114(Pt 13):2501-11 PubMed
Mol Cell. 2013 Sep 26;51(6):737-50 PubMed
J Cell Sci. 2013 Jun 15;126(Pt 12):2730-9 PubMed
Exp Cell Res. 1996 Aug 25;227(1):33-9 PubMed
J Lipid Res. 2007 Mar;48(3):726-32 PubMed
Mol Biol Cell. 1998 Dec;9(12):3547-60 PubMed
Biochem J. 2001 Aug 1;357(Pt 3):905-10 PubMed
Mol Cell Proteomics. 2011 Feb;10(2):M110.003376 PubMed
Biochem J. 1987 Dec 15;248(3):765-70 PubMed
FEBS J. 2013 Dec;280(24):6295-310 PubMed
Proc Natl Acad Sci U S A. 2012 Jun 26;109(26):10581-6 PubMed
FEBS Lett. 2000 May 12;473(2):222-6 PubMed
Cell. 2003 Jul 11;114(1):99-111 PubMed
Biochem J. 1998 Oct 1 ;335 ( Pt 1):139-46 PubMed
Mol Cell. 2005 May 13;18(4):435-45 PubMed
Biochim Biophys Acta. 2015 Jun;1851(6):746-58 PubMed
J Histochem Cytochem. 1995 Feb;43(2):181-91 PubMed
Proc Natl Acad Sci U S A. 2014 Oct 21;111(42):15054-9 PubMed
Proc Natl Acad Sci U S A. 2005 Sep 13;102(37):13052-7 PubMed
J Cell Biol. 1998 Oct 19;143(2):501-10 PubMed
Biochem J. 1997 Oct 15;327 ( Pt 2):569-76 PubMed
Curr Biol. 1998 Mar 12;8(6):343-6 PubMed
Mol Cell. 2004 Mar 12;13(5):677-88 PubMed
Anal Biochem. 2002 Feb 15;301(2):243-54 PubMed
Chem Phys Lipids. 2012 Feb;165(2):207-15 PubMed
J Cell Sci. 2006 Dec 15;119(Pt 24):5160-8 PubMed
J Biol Chem. 2007 Nov 2;282(44):32093-105 PubMed
J Biol Chem. 1998 Jan 2;273(1):417-24 PubMed
Adv Enzyme Regul. 2011;51(1):91-9 PubMed
Biochim Biophys Acta. 1993 Oct 7;1179(1):27-75 PubMed
Curr Protoc Cell Biol. 2009 Mar;Chapter 24:Unit 24.4 PubMed
Nature. 1998 Jul 30;394(6692):432-3 PubMed
Mol Biol Cell. 2001 Jun;12(6):1633-44 PubMed
J Biol Chem. 2004 Oct 22;279(43):44683-9 PubMed
Proc Natl Acad Sci U S A. 2007 Oct 23;104(43):16834-9 PubMed
Biochem J. 2009 Aug 27;422(3):473-82 PubMed
EMBO J. 2004 Oct 13;23(20):3995-4006 PubMed
Cell Rep. 2012 Sep 27;2(3):462-9 PubMed
Cell Rep. 2014 Feb 13;6(3):578-91 PubMed
Biochem J. 2002 May 1;363(Pt 3):657-66 PubMed
Physiol Rev. 2013 Jul;93(3):1019-137 PubMed
Mol Cell. 1998 Jul;2(1):157-62 PubMed
Biochem J. 2011 Nov 1;439(3):391-401 PubMed
Biochem J. 2004 Feb 1;377(Pt 3):653-63 PubMed
J Cell Sci. 2015 Nov 15;128(22):4047-56 PubMed
Proc Natl Acad Sci U S A. 2008 Jun 24;105(25):8649-54 PubMed
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