A high phosphorylation state and increased activity of the TRE motif in the NIH3T3 cell transformant induced by retTPC

Yukihito Ishizaka; Masahide Takahashi; Toshikazu Ushijima; Takashi Sugimura; Minako Nagao

doi:10.1016/0006-291X(91)91719-S

A high phosphorylation state and increased activity of the TRE motif in the NIH3T3 cell transformant induced by ret^TPC

Yukihito Ishizaka
, Masahide Takahashi
, Toshikazu Ushijima
, Takashi Sugimura
, Minako Nagao

Research output: Contribution to journal › Article › peer-review

5 Citations (Scopus)

Abstract

A 57 kDa protein was detected in an NIH3T3 transformant induced by ret^TPC, 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 ret^TPC 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 ret^TPC product affects the cellular serine/threonine phosphorylation state resulting in high phosphorylation of c-jun protein.

Original language	English
Pages (from-to)	1331-1336
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	179
Issue number	3
DOIs	https://doi.org/10.1016/0006-291X(91)91719-S
Publication status	Published - 30-09-1991
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0006-291X(91)91719-S

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@article{0c1d5ab3dbbb4409a6f41c595f5d14d2,

title = "A high phosphorylation state and increased activity of the TRE motif in the NIH3T3 cell transformant induced by retTPC",

abstract = "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.",

author = "Yukihito Ishizaka and Masahide Takahashi and Toshikazu Ushijima and Takashi Sugimura and Minako Nagao",

note = "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.",

year = "1991",

month = sep,

day = "30",

doi = "10.1016/0006-291X(91)91719-S",

language = "English",

volume = "179",

pages = "1331--1336",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Elsevier B.V.",

number = "3",

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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.

UR - https://www.scopus.com/pages/publications/0025940075

UR - https://www.scopus.com/pages/publications/0025940075#tab=citedBy

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 -

A high phosphorylation state and increased activity of the TRE motif in the NIH3T3 cell transformant induced by ret^TPC

Abstract

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