Premium
Interaction of ADP‐ribosylated actin with actin binding proteins
Author(s) -
Ballweber Edda,
Galla Marco,
Aktories Klaus,
Yeoh Sharon,
Weeds Alan G.,
Mannherz Hans Georg
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03040-x
Subject(s) - gelsolin , actin binding protein , actin , microfilament , actin remodeling , mdia1 , cofilin , myosin , chemistry , fascin , biophysics , microbiology and biotechnology , biochemistry , biology , actin cytoskeleton , cytoskeleton , cell
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 native actin, indicating that its ability to take part in normal subunit interactions within filaments is not fully eliminated. We also show that ADP‐ribosylated actin forms antiparallel but not parallel dimers: the former are not able to form filaments. ADP‐ribosylated actin interacts with deoxyribonuclease I, vitamin D binding protein, thymosin β 4 , cofilin and gelsolin segment 1 like native actin. Interaction with myosin subfragment 1 revealed that the potential of the modified actin to aggregate into oligomers or short filaments is not fully eliminated.