Interaction of ADP-ribosylated actin with actin binding proteins

Actin ADP-ribosylated at Arg177 was previously shown not to polymerise after increasing the ionic strength, but to cap the barbed ends of filaments. Here we confirm that the polymerisation of ADP-ribosylated actin is inhibited, however, under specific conditions the modified actin copolymerises with...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	FEBS letters 2001-11, Vol.508 (1), p.131-135
Hauptverfasser:	Ballweber, Edda, Galla, Marco, Aktories, Klaus, Yeoh, Sharon, Weeds, Alan G., Mannherz, Hans Georg
Format:	Artikel
Sprache:	eng
Schlagworte:	1,4-PBM, 1,4-phenylene-bismaleimide Actin binding protein Actin Depolymerizing Factors Actins - chemistry Actins - metabolism Adenosine Diphosphate Ribose - metabolism ADP-ribosylated actin Animals Dansyl Compounds - metabolism DbP, vitamin D binding protein DNase I, deoxyribonuclease I (EC 3.1.21.1.) EDC, 1-ethyl-3[3(dimethylamino)propyl] carbodiimide Electrophoresis, Polyacrylamide Gel FFD, 1,5-difluoro-2,4-dinitrobenzene Gelsolin - metabolism Humans Indicators and Reagents - metabolism LD, lower dimer of actin Microfilament Proteins - metabolism Muscle, Skeletal - chemistry NAD, nicotinamide adenindinucleotide Polymers - chemistry Polymers - metabolism Rabbits Tβ4, thymosin β4
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!