Lifeact: a versatile marker to visualize F-actin

被引：1624

作者：

Riedl, Julia ^{[2
]}

Crevenna, Alvaro H. ^{[2
]}

Kessenbrock, Kai ^{[3
]}

Yu, Jerry Haochen ^{[2
]}

Neukirchen, Dorothee ^{[4
]}

Bista, Michal

Bradke, Frank ^{[4
]}

Jenne, Dieter ^{[3
]}

Holak, Tad A. ^{[5
]}

Werb, Zena ^{[6
,7
]}

Sixt, Michael ^{[1
]}

Wedlich-Soldner, Roland ^{[2
]}

机构：

[1] Max Planck Inst Biochem, Dept Mol Med, D-82152 Martinsried, Germany

[2] Max Planck Inst Biochem, Independent Jr Res Grp Cellular Dynam & Cell Patt, D-82152 Martinsried, Germany

[3] Max Planck Inst Neurobiol, Dept Neuroimmunol, D-82152 Martinsried, Germany

[4] Max Planck Inst Neurobiol, Independent Jr Res Grp Axonal Growth & Regenerat, D-82152 Martinsried, Germany

[5] Max Planck Inst Biochem, Dept Struct Cell Biol, D-82152 Martinsried, Germany

[6] Univ Calif San Francisco, Dept Anat, San Francisco, CA 94143 USA

[7] Univ Calif San Francisco, Program Biomed Sci, San Francisco, CA 94143 USA

来源：

NATURE METHODS | 2008年 / 5卷 / 07期

关键词：

D O I：

10.1038/nmeth.1220

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Live imaging of the actin cytoskeleton is crucial for the study of many fundamental biological processes, but current approaches to visualize actin have several limitations. Here we describe Lifeact, a 17-amino-acid peptide, which stained filamentous actin (F-actin) structures in eukaryotic cells and tissues. Lifeact did not interfere with actin dynamics in vitro and in vivo and in its chemically modified peptide form allowed visualization of actin dynamics in nontransfectable cells.

引用

页码：605 / 607

页数：3

共 15 条

[1] Isolation and characterization of a novel actin filament-binding protein from Saccharomyces cerevisiae [J].

Asakura, T ;

Sasaki, T ;

Nagano, F ;

Satoh, A ;

Obaishi, H ;

Nishioka, H ;

Imamura, H ;

Hotta, K ;

Tanaka, K ;

Nakanishi, H ;

Takai, Y .

ONCOGENE, 1998, 16 (01) :121-130

[2] Dynamic actin patterns and Arp2/3 assembly at the substrate-attached surface of motile cells [J].

Bretschneider, T ;

Diez, S ;

Anderson, K ;

Heuser, J ;

Clarke, M ;

Müller-Taubenberger, A ;

Köhler, J ;

Gerisch, G .

CURRENT BIOLOGY, 2004, 14 (01) :1-10

[3] Versatile fluorescent probes for actin filaments based on the actin-binding domain of Utrophin [J].

Burkel, Brian M. ;

von Dassow, George ;

Bement, William M. .

CELL MOTILITY AND THE CYTOSKELETON, 2007, 64 (11) :822-832

[4] PYRENE ACTIN - DOCUMENTATION OF THE VALIDITY OF A SENSITIVE ASSAY FOR ACTIN POLYMERIZATION [J].

COOPER, JA ;

WALKER, SB ;

POLLARD, TD .

JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY, 1983, 4 (02) :253-262

[5] CONFORMATION OF THYMOSIN BETA(4) IN WATER DETERMINED BY NMR-SPECTROSCOPY [J].

CZISCH, M ;

SCHLEICHER, M ;

HORGER, S ;

VOELTER, W ;

HOLAK, TA .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 1993, 218 (02) :335-344

[6] GFP-moesin illuminates actin cytoskeleton dynamics in living tissue and demonstrates cell shape changes during morphogenesis in Drosophila [J].

Edwards, KA ;

Demsky, M ;

Montague, RA ;

Weymouth, N ;

Kiehart, DP .

DEVELOPMENTAL BIOLOGY, 1997, 191 (01) :103-117

[7] Visualizing cytoskeleton dynamics in mammalian cells using a humanized variant of monomeric red fluorescent protein [J].

Fischer, M ;

Haase, I ;

Wiesner, S ;

Müller-Taubenberger, A .

FEBS LETTERS, 2006, 580 (10) :2495-2502

[8] A contractile nuclear actin network drives chromosome congression in oocytes [J].

Lénárt, P ;

Bacher, CP ;

Daigle, N ;

Hand, AR ;

Eils, R ;

Terasaki, M ;

Ellenberg, J .

NATURE, 2005, 436 (7052) :812-818

[9] A METHOD FOR INCORPORATING MACROMOLECULES INTO ADHERENT CELLS [J].

MCNEIL, PL ;

MURPHY, RF ;

LANNI, F ;

TAYLOR, DL .

JOURNAL OF CELL BIOLOGY, 1984, 98 (04) :1556-1564

[10] Use of a fusion protein between GFP and an anti-binding domain to visualize transient filamentous-actin structures [J].

Pang, KM ;

Lee, E ;

Knecht, DA .

CURRENT BIOLOGY, 1998, 8 (07) :405-408

← 1 2 →