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Title: The carboxyl terminal tyrosine 417 residue of NOK has an autoinhibitory effect on NOK-mediated signaling transductions

Abstract

Receptor protein tyrosine kinases (RPTKs) are essential mediators of cell growth, differentiation, migration, and metabolism. Recently, a novel RPTK named NOK has been cloned and characterized. In current study, we investigated the role of the carboxyl terminal tyrosine 417 residue of NOK in the activations of different signaling pathways. A single tyrosine to phenylalanine point mutation at Y417 site (Y417 F) not only dramatically enhanced the NOK-induced activation of extracellular signal-regulated kinase (ERK), but also markedly promoted the NOK-mediated activation of both signal transducer and activator of transcription 1 and 3 (STAT1 and 3). Moreover, the proliferation potential of NIH3T3-NOK (Y417F) stable cells were significantly elevated as compared with that of NIH3T3-NOK. Overall, our results demonstrate that the tyrosine Y417 residue at the carboxyl tail of NOK exhibits an autoinhibitory role in NOK-mediated signaling transductions.

Authors:
 [1];  [1];  [1];  [1];  [1];  [1];  [1];  [2]
  1. Tsinghua Institute of Genome Research, Institute of Biomedicine and School of Medicine, Tsinghua University, Beijing 100084 (China)
  2. Tsinghua Institute of Genome Research, Institute of Biomedicine and School of Medicine, Tsinghua University, Beijing 100084 (China) and Department of Microbiology and Etiology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing 100005 (China). E-mail: Liu_Li@mail.tsinghua.edu.cn
Publication Date:
OSTI Identifier:
20991323
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 356; Journal Issue: 2; Other Information: DOI: 10.1016/j.bbrc.2007.02.154; PII: S0006-291X(07)00455-X; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; CELL PROLIFERATION; GENE MUTATIONS; METABOLISM; NITRIC OXIDE; PHENYLALANINE; PHOSPHOTRANSFERASES; RECEPTORS; TRANSCRIPTION; TYROSINE

Citation Formats

Li Yinghua, Zhong Shan, Rong Zhili, Ren Yongming, Li Zhiyong, Zhang Shuping, Chang Zhijie, and Liu Li. The carboxyl terminal tyrosine 417 residue of NOK has an autoinhibitory effect on NOK-mediated signaling transductions. United States: N. p., 2007. Web.
Li Yinghua, Zhong Shan, Rong Zhili, Ren Yongming, Li Zhiyong, Zhang Shuping, Chang Zhijie, & Liu Li. The carboxyl terminal tyrosine 417 residue of NOK has an autoinhibitory effect on NOK-mediated signaling transductions. United States.
Li Yinghua, Zhong Shan, Rong Zhili, Ren Yongming, Li Zhiyong, Zhang Shuping, Chang Zhijie, and Liu Li. Fri . "The carboxyl terminal tyrosine 417 residue of NOK has an autoinhibitory effect on NOK-mediated signaling transductions". United States. doi:.
@article{osti_20991323,
title = {The carboxyl terminal tyrosine 417 residue of NOK has an autoinhibitory effect on NOK-mediated signaling transductions},
author = {Li Yinghua and Zhong Shan and Rong Zhili and Ren Yongming and Li Zhiyong and Zhang Shuping and Chang Zhijie and Liu Li},
abstractNote = {Receptor protein tyrosine kinases (RPTKs) are essential mediators of cell growth, differentiation, migration, and metabolism. Recently, a novel RPTK named NOK has been cloned and characterized. In current study, we investigated the role of the carboxyl terminal tyrosine 417 residue of NOK in the activations of different signaling pathways. A single tyrosine to phenylalanine point mutation at Y417 site (Y417 F) not only dramatically enhanced the NOK-induced activation of extracellular signal-regulated kinase (ERK), but also markedly promoted the NOK-mediated activation of both signal transducer and activator of transcription 1 and 3 (STAT1 and 3). Moreover, the proliferation potential of NIH3T3-NOK (Y417F) stable cells were significantly elevated as compared with that of NIH3T3-NOK. Overall, our results demonstrate that the tyrosine Y417 residue at the carboxyl tail of NOK exhibits an autoinhibitory role in NOK-mediated signaling transductions.},
doi = {},
journal = {Biochemical and Biophysical Research Communications},
number = 2,
volume = 356,
place = {United States},
year = {Fri May 04 00:00:00 EDT 2007},
month = {Fri May 04 00:00:00 EDT 2007}
}