Mechanism of interaction of Acanthamoeba actophorin (ADF/cofilin) with actin filaments

被引:244
作者
Blanchoin, L [1 ]
Pollard, TD [1 ]
机构
[1] Salk Inst Biol Studies, Struct Biol Lab, La Jolla, CA 92037 USA
关键词
D O I
10.1074/jbc.274.22.15538
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We characterized the interaction of Acanthamoeba actophorin, a member of ADF/cofilin family, with filaments of amoeba and rabbit skeletal muscle actin. The affinity is about 10 times higher for muscle actin filaments (K-d = 0.5 mu M) than amoeba actin filaments (K-d = 5 mu M) even though the affinity for muscle and amoeba Mg-ADP-actin monomers (K-d = 0.1 mu M) is the same (Blanchoin, L., and Pollard, T. D. (1998) J, Biol, Chem. 273, 25106-25111), Actophorin binds slowly (k(+) = 0.03 mu M-1 s(-1)) to and dissociates from amoeba actin filaments in a simple bimolecular reaction, but binding to muscle actin filaments is cooperative. Actophorin severs filaments in a concentration-dependent fashion. Phosphate or BeF3 bound to ADP-actin filaments inhibit actophorin binding. Actophorin increases the rate of phosphate release from actin filaments more than 10-fold. The time course of the interaction of actophorin with filaments measured by quenching of the fluorescence of pyrenyl-actin or fluorescence anisotropy of rhodamine-actophorin is complicated, because severing, depolymerization, and repolymerization follows binding. The 50-fold higher affinity of actophorin for Mg-ADP-actin monomers (K-d = 0.1 mu M) than ADP-actin filaments provides the thermodynamic basis for driving disassembly of filaments that have hydrolyzed ATP and dissociated gamma-phosphate.
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页码:15538 / 15546
页数:9
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共 51 条
[21]  
KOUYAMA T, 1981, EUR J BIOCHEM, V114, P33
[22]   THE KINETICS OF THE INTERACTION BETWEEN THE ACTIN-BINDING DOMAIN OF ALPHA-ACTININ AND F-ACTIN [J].
KUHLMAN, PA ;
ELLIS, J ;
CRITCHLEY, DR ;
BAGSHAW, CR .
FEBS LETTERS, 1994, 339 (03) :297-301
[23]   Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis [J].
Lappalainen, P ;
Fedorov, EV ;
Fedorov, AA ;
Almo, SC ;
Drubin, DG .
EMBO JOURNAL, 1997, 16 (18) :5520-5530
[24]   AN ACTIN-DEPOLYMERIZING PROTEIN (DEPACTIN) FROM STARFISH OOCYTES - PROPERTIES AND INTERACTION WITH ACTIN [J].
MABUCHI, I .
JOURNAL OF CELL BIOLOGY, 1983, 97 (05) :1612-1621
[25]   CHARACTERIZATION OF ACTIN FILAMENT SEVERING BY ACTOPHORIN FROM ACANTHAMOEBA-CASTELLANII [J].
MACIVER, SK ;
ZOT, HG ;
POLLARD, TD .
JOURNAL OF CELL BIOLOGY, 1991, 115 (06) :1611-1620
[26]   The effect of two actin depolymerizing factors (ADF/cofilins) on actin filament turnover:: pH sensitivity of F-actin binding by human ADF, but not of Acanthamoeba actophorin [J].
Maciver, SK ;
Pope, BJ ;
Whytock, S ;
Weeds, AG .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1998, 256 (02) :388-397
[27]   How ADF/cofilin depolymerizes actin filaments - Commentary [J].
Maciver, SK .
CURRENT OPINION IN CELL BIOLOGY, 1998, 10 (01) :140-144
[28]   MECHANISM OF ACTION OF CYTOCHALASIN-B ON ACTIN [J].
MACLEANFLETCHER, S ;
POLLARD, TD .
CELL, 1980, 20 (02) :329-341
[29]  
MAEKAWA S, 1984, J BIOCH, V95, P337
[30]   Cofilin changes the twist of F-actin: Implications for actin filament dynamics and cellular function [J].
McGough, A ;
Pope, B ;
Chiu, W ;
Weeds, A .
JOURNAL OF CELL BIOLOGY, 1997, 138 (04) :771-781