scholarly journals A KH Domain-Containing Putative RNA-Binding Protein Is Critical for Heat Stress-Responsive Gene Regulation and Thermotolerance in Arabidopsis

2013 ◽  
Vol 6 (2) ◽  
pp. 386-395 ◽  
Author(s):  
Qingmei Guan ◽  
Changlong Wen ◽  
Haitao Zeng ◽  
Jianhua Zhu
Keyword(s):  
Gene Regulation ◽  
Heat Stress ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Kh Domain ◽  
Responsive Gene

Cold-induced RNA-binding protein (CIRBP) regulates the expression of Src-associated during mitosis of 68 kDa (Sam68) and extracellular signal-regulated kinases (ERK) during heat stress-induced testicular injury

2020 ◽  
Vol 32 (18) ◽  
pp. 1357
Author(s):  
Chengcheng Xu ◽  
Dandan Ke ◽  
Liping Zou ◽  
Nianyu Li ◽  
Yingying Wang ◽  
...  
Keyword(s):  
Gene Expression ◽  
Heat Stress ◽  
Protein Expression ◽  
Rna Binding ◽  
Cell Model ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Protein Levels ◽  
Extracellular Signal ◽  
Testicular Injury

In this study, the ability of cold-induced RNA-binding protein (CIRBP) to regulate the expression of Src-associated during mitosis of 68 kDa (Sam68) and extracellular signal-regulated kinases (ERK) in the mouse testis and mouse primary spermatocytes (GC-2spd cell line) before and after heat stress was examined to explore the molecular mechanism by which CIRBP decreases testicular injury. A mouse testicular hyperthermia model, a mouse primary spermatocyte hyperthermia model and a low CIRBP gene-expression cell model were constructed and their relevant parameters were analysed. The mRNA and protein levels of CIRBP and Sam68 were significantly decreased in the 3-h and 12-h testicular heat-stress groups, extracellular signal-regulated kinase 1/2 (ERK1/2) protein expression was not significantly affected but phospho-ERK1/2 protein levels were significantly decreased. GC-2spd cellular heat-stress results showed that the mRNA and protein concentrations of CIRBP and Sam68 were reduced 48h after heat stress. In the low CIRBP gene-expression cell model, CIRBP protein expression was significantly decreased. Sam68 mRNA expression was significantly decreased only at the maximum transfection concentration of 50nM and Sam68 protein expression was not significantly affected. These findings suggest that CIRBP may regulate the expression of Sam68 at the transcriptional level and the expression of phospho-ERK1/2 protein, both of which protect against heat-stress-induced testicular injury in mice.

scholarly journals The Arabidopsis KH-Domain RNA-Binding Protein ESR1 Functions in Components of Jasmonate Signalling, Unlinking Growth Restraint and Resistance to Stress

PLoS ONE ◽  
2015 ◽  
Vol 10 (5) ◽  
pp. e0126978 ◽  
Author(s):  
Louise F. Thatcher ◽  
Lars G. Kamphuis ◽  
James K. Hane ◽  
Luis Oñate-Sánchez ◽  
Karam B. Singh
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Kh Domain ◽  
Resistance To Stress ◽  
Jasmonate Signalling

scholarly journals Role of the RNA-Binding Protein Tristetraprolin in Glucocorticoid-Mediated Gene Regulation

2008 ◽  
Vol 180 (12) ◽  
pp. 8342-8353 ◽  
Author(s):  
Faoud T. Ishmael ◽  
Xi Fang ◽  
Maria Rosaria Galdiero ◽  
Ulus Atasoy ◽  
William F. C. Rigby ◽  
...  
Keyword(s):  
Gene Regulation ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein

scholarly journals The RNA-binding protein Sam68 is a multifunctional player in human cancer

2011 ◽  
Vol 18 (4) ◽  
pp. R91-R102 ◽  
Author(s):  
Pamela Bielli ◽  
Roberta Busà ◽  
Maria Paola Paronetto ◽  
Claudio Sette
Keyword(s):  
Nuclear Export ◽  
Rna Binding ◽  
Viral Infections ◽  
Human Cancer ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Mrna Translation ◽  
Endocrine Tumors ◽  
Recent Advancement ◽  
Kh Domain

Src associated in mitosis, of 68 kDa (Sam68) is a KH domain RNA-binding protein that belongs to the signal transduction and activation of RNA family. Although ubiquitously expressed, Sam68 plays very specialized roles in different cellular environments. In most cells, Sam68 resides in the nucleus and is involved in several steps of mRNA processing, from transcription, to alternative splicing, to nuclear export. In addition, Sam68 translocates to the cytoplasm upon cell stimulation, cell cycle transitions or viral infections, where it takes part to signaling complexes and associates with the mRNA translation machinery. Recent evidence has linked Sam68 function to the onset and progression of endocrine tumors, such as prostate and breast carcinomas. Notably, all the biochemical activities reported for Sam68 seem to be implicated in carcinogenesis. Herein, we review the recent advancement in the knowledge of Sam68 function and regulation and discuss it in the frame of its participation to neoplastic transformation and tumor progression.

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