TY - JOUR
T1 - Drebrin, a development-associated brain protein from rat embryo, causes the dissociation of tropomyosin from actin filaments
AU - Ishikawa, Ryoki
AU - Hayashi, Kensuke
AU - Shirao, Tomoaki
AU - Xue, Yinhuan
AU - Takagi, Takashi
AU - Sasaki, Yo
AU - Kohama, Kazuhiro
PY - 1994/11/25
Y1 - 1994/11/25
N2 - Drebrin is a development-associated neuroprotein whose cDNA into fibroblasts causes the formation of dendrite-like structures (Shirao, T., Kojima, N., and Obata, K. (1992) Neuroreport 3, 109-112). To explore molecular functions of drebrin during brain development, we purified drebrin from brains of rat embryos. Drebrin bound to actin filaments at a stoichiometry of 1:5 with a dissociation constant (K(d) of 1.2 x 10-7 M. It strongly inhibited the actin binding activity of tropomyosin. Excess amounts of tropomyosin also inhibited the drebrin binding to actin filaments, suggesting that drebrin and tropomyosin competitively bind to actin filaments. Further, drebrin inhibited not only the actin binding activity of α-actinin but also the actin cross-linking activity of α-actinin. Gene transfection experiments revealed that tropomyosin was dissociated from actin filaments in drebrin-overexpressing fibroblasts. Thus we hypothesize that drebrin may destabilize actin filaments by dissociating tropomyosin and α- actinin from actin filaments, resulting in the formation of axon and dendrites during neuronal development.
AB - Drebrin is a development-associated neuroprotein whose cDNA into fibroblasts causes the formation of dendrite-like structures (Shirao, T., Kojima, N., and Obata, K. (1992) Neuroreport 3, 109-112). To explore molecular functions of drebrin during brain development, we purified drebrin from brains of rat embryos. Drebrin bound to actin filaments at a stoichiometry of 1:5 with a dissociation constant (K(d) of 1.2 x 10-7 M. It strongly inhibited the actin binding activity of tropomyosin. Excess amounts of tropomyosin also inhibited the drebrin binding to actin filaments, suggesting that drebrin and tropomyosin competitively bind to actin filaments. Further, drebrin inhibited not only the actin binding activity of α-actinin but also the actin cross-linking activity of α-actinin. Gene transfection experiments revealed that tropomyosin was dissociated from actin filaments in drebrin-overexpressing fibroblasts. Thus we hypothesize that drebrin may destabilize actin filaments by dissociating tropomyosin and α- actinin from actin filaments, resulting in the formation of axon and dendrites during neuronal development.
UR - http://www.scopus.com/inward/record.url?scp=0028139040&partnerID=8YFLogxK
M3 - Article
C2 - 7961990
AN - SCOPUS:0028139040
SN - 0021-9258
VL - 269
SP - 29928
EP - 29933
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 47
ER -