FEBS Lett 2001,
PMID: 11707283
Ballweber, E; Galla, M; Aktories, K; Yeoh, S; Weeds, A G; Mannherz, H G
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 beta(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.
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Text Mining Data
Dashed line = No text mining data
Manually curated Databases
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IRef Hprd Interaction:
MYL1
—
ACTA2
(in vitro)
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IRef Hprd Interaction:
ACTA1
—
CFL1
(in vitro)
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IRef Hprd Interaction:
ACTA1
—
CFL1
(two hybrid)
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IRef Hprd Interaction:
ACTA1
—
DNASE1
(in vivo)
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IRef Hprd Interaction:
ACTA1
—
DNASE1
(in vitro)
-
IRef Hprd Interaction:
DNASE1
—
ACTA2
(in vitro)
-
IRef Hprd Interaction:
ACTA2
—
CFL1
(in vitro)
-
IRef Hprd Interaction:
ACTA1
—
MYL1
(in vitro)
-
IRef Ophid Interaction:
MYL1
—
ACTA2
(aggregation, confirmational text mining)
-
IRef Ophid Interaction:
ACTA1
—
DNASE1
(aggregation, confirmational text mining)
-
IRef Ophid Interaction:
DNASE1
—
ACTA2
(aggregation, confirmational text mining)
-
IRef Ophid Interaction:
ACTA1
—
MYL1
(aggregation, confirmational text mining)
In total, 6 gene pairs are associated to this article in curated databases