TY - JOUR
T1 - Domain-specific phosphorylation of vimentin and glial fibrillary acidic protein by PKN
AU - Matsuzawa, Kaori
AU - Kosako, Hidetaka
AU - Inagaki, Naoyuki
AU - Shibata, Hideki
AU - Mukai, Hideyuki
AU - Ono, Yoshitaka
AU - Amano, Mutsuki
AU - Kaibuchi, Kozo
AU - Matsuura, Yoshiharu
AU - Azuma, Ichiro
AU - Inagaki, Masaki
N1 - Funding Information:
We are grateful to Y. Nishi and H. Goto for assistance with the electron microscopy and two-dimensional tryptic phosphopeptide mapping. M. Ohara provided critical comments on the manuscript and K. Kuromiya provided secretarial assistance. This research was supported in part by Grants-in-Aid for Scienti®c Research and Cancer Research from the Ministry of Education, Science, Sports and Culture of Japan, and special coordination funds from JST, Science and Technology Agency of Japan.
PY - 1997/5/29
Y1 - 1997/5/29
N2 - PKN is a serine/threonine protein kinase with a catalytic domain homologous to the protein kinase C family and unique N-terminal leucine zipper-like sequences. Using analyses with the yeast two-hybrid system and in vitro binding assay, we found that the regulatory domain of PKN interacted with vimentin. We then examined whether PKN would phosphorylate vimentin in vitro. Vimentin proved to be an excellent substrate for PKN, and the phosphorylation of vimentin by PKN occurred in the head domain with the result of a nearly complete inhibition of its filament formation in vitro. Similar results were also obtained with another type III intermediate filament protein, glial fibrillary acidic protein (GFAP). These results raise the possibility that PKN may regulate filament structures of vimentin and GFAP by domain-specific phosphorylation.
AB - PKN is a serine/threonine protein kinase with a catalytic domain homologous to the protein kinase C family and unique N-terminal leucine zipper-like sequences. Using analyses with the yeast two-hybrid system and in vitro binding assay, we found that the regulatory domain of PKN interacted with vimentin. We then examined whether PKN would phosphorylate vimentin in vitro. Vimentin proved to be an excellent substrate for PKN, and the phosphorylation of vimentin by PKN occurred in the head domain with the result of a nearly complete inhibition of its filament formation in vitro. Similar results were also obtained with another type III intermediate filament protein, glial fibrillary acidic protein (GFAP). These results raise the possibility that PKN may regulate filament structures of vimentin and GFAP by domain-specific phosphorylation.
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U2 - 10.1006/bbrc.1997.6669
DO - 10.1006/bbrc.1997.6669
M3 - Article
C2 - 9175763
AN - SCOPUS:0031589968
SN - 0006-291X
VL - 234
SP - 621
EP - 625
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -