TY - JOUR
T1 - A high phosphorylation state and increased activity of the TRE motif in the NIH3T3 cell transformant induced by retTPC
AU - Ishizaka, Yukihito
AU - Takahashi, Masahide
AU - Ushijima, Toshikazu
AU - Sugimura, Takashi
AU - Nagao, Minako
N1 - Funding Information:
Acknowledgments: We are grateful to Dr. R. Bravo for providing a mouse c-jun cDNA clone and Dr. R. Tjian for the CAT constructs, pUCAT and pX8CAT. We are also grateful to Dr. Kominami for a mouse rDNA clone and Dr. Mulligan for providing a DO1 vector. We thank Dr. Nomura (Nippon Veterinary and Zootechnological College) for providing m-B and -D cDNA probes. This study was supported by a Grant-in-Aid from the Ministry of Health and Welfare of Japan for a Comprehensive lo-Year Strategy for Cancer Control.
PY - 1991/9/30
Y1 - 1991/9/30
N2 - A 57 kDa protein was detected in an NIH3T3 transformant induced by retTPC, an activated form of the ret proto-oncogene which encodes a receptor-tyrosine kinase. A high phosphorylation state and increased activity of a TPA responsive element was observed in the transformant. Increased expression of c-jun mRNA was also detected. A 40 kDa protein in the retTPC transformant, which was specifically immunoprecipitable with v-jun antiserum, was highly phosphorylated mainly at a serine residue(s). These data suggest that an aberrant signal triggered by a retTPC product affects the cellular serine/threonine phosphorylation state resulting in high phosphorylation of c-jun protein.
AB - A 57 kDa protein was detected in an NIH3T3 transformant induced by retTPC, an activated form of the ret proto-oncogene which encodes a receptor-tyrosine kinase. A high phosphorylation state and increased activity of a TPA responsive element was observed in the transformant. Increased expression of c-jun mRNA was also detected. A 40 kDa protein in the retTPC transformant, which was specifically immunoprecipitable with v-jun antiserum, was highly phosphorylated mainly at a serine residue(s). These data suggest that an aberrant signal triggered by a retTPC product affects the cellular serine/threonine phosphorylation state resulting in high phosphorylation of c-jun protein.
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U2 - 10.1016/0006-291X(91)91719-S
DO - 10.1016/0006-291X(91)91719-S
M3 - Article
C2 - 1930177
AN - SCOPUS:0025940075
SN - 0006-291X
VL - 179
SP - 1331
EP - 1336
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -