TY - JOUR
T1 - Rho-associated kinase phosphorylates desmin, the myogenic intermediate filament protein, at unique amino-terminal sites
AU - Inada, Hiroyasu
AU - Goto, Hidemasa
AU - Tanabe, Kazushi
AU - Nishi, Yoshimi
AU - Kaibuchi, Kozo
AU - Inagaki, Masaki
N1 - Funding Information:
This work was supported in part by Grants-in-Aid for Scientific Research and Cancer Research from the Ministry of Education, Science, Sports, and Culture of Japan; Japan Society of the Promotion of Science Research for the Future; special coordination funds from the Science and Technology Agency of the Government of Japan; and a grant from Bristol–Myers–Squibb. We thank K. Ku-romiya for secretarial assistance, K. Hara for technical assistance, and M. Ohara for critique of the manuscript.
PY - 1998/12/9
Y1 - 1998/12/9
N2 - We obtained evidence that Rho-associated kinase (Rho-kinase) phosphorylates desmin, the myogenic intermediate filament protein, with approximately 2 mol phosphate per mole of desmin in vitro. Desmin phosphorylated by Rho-kinase lost the potential to form 10-nm filaments. Thr-16, Thr-75, and Thr-76 on desmin proved to be the major phosphorylation sites for Rho-kinase. All these sites are located within the head domain and are different from the reported phosphorylation sites of protein kinase A, protein kinase C, and cdc2 kinase. We are entertaining the notion that Rho-kinase may regulate filament structures of desmin by site-specific phosphorylation.
AB - We obtained evidence that Rho-associated kinase (Rho-kinase) phosphorylates desmin, the myogenic intermediate filament protein, with approximately 2 mol phosphate per mole of desmin in vitro. Desmin phosphorylated by Rho-kinase lost the potential to form 10-nm filaments. Thr-16, Thr-75, and Thr-76 on desmin proved to be the major phosphorylation sites for Rho-kinase. All these sites are located within the head domain and are different from the reported phosphorylation sites of protein kinase A, protein kinase C, and cdc2 kinase. We are entertaining the notion that Rho-kinase may regulate filament structures of desmin by site-specific phosphorylation.
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U2 - 10.1006/bbrc.1998.9732
DO - 10.1006/bbrc.1998.9732
M3 - Article
C2 - 9875213
AN - SCOPUS:0007354630
SN - 0006-291X
VL - 253
SP - 21
EP - 25
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -