An ABA-regulated putative RNA-binding protein affects seed germination of Arabidopsis under ABA or abiotic stress conditions

Cold-inducible RNA-binding protein (CIRP) is an intracellular stress-response protein that can respond to various stress conditions by changing its expression and regulating mRNA stability. As an RNA-binding protein, CIRP modulates gene expression at the post-transcriptional level, including those genes involved in DNA repair, cellular redox metabolism, circadian rhythms, telomere maintenance, and cell survival. CIRP is expressed in a large variety of tissues, including testis, brain, lung, kidney, liver, stomach, bone marrow, and heart. Recent studies have observed the important role of CIRP in cardiac physiology and diseases. CIRP regulates cardiac electrophysiological properties such as the repolarization of cardiomyocytes, the susceptibility of atrial fibrillation, and the function of the sinoatrial node in response to stress. CIRP has also been suggested to protect cardiomyocytes from apoptosis under various stress conditions, including heart failure, high glucose conditions, as well as during extended heart preservation under hypothermic conditions. This review summarizes the findings of CIRP investigations in cardiac physiology and diseases and the underlying molecular mechanism.

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OsDEG10 encoding a small RNA-binding protein is involved in abiotic stress signaling

Biochemical and Biophysical Research Communications ◽

10.1016/j.bbrc.2009.01.131 ◽

2009 ◽

Vol 380 (3) ◽

pp. 597-602 ◽

Cited By ~ 17

Author(s):

Hee-Yeon Park ◽

In Soon Kang ◽

Ji-Sung Han ◽

Choon-Hwan Lee ◽

Gynheung An ◽

...

Keyword(s):

Abiotic Stress ◽

Small Rna ◽

Rna Binding ◽

Binding Protein ◽

Rna Binding Protein ◽

Stress Signaling

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Zinc finger-containing glycine-rich RNA-binding protein inOryza sativahas an RNA chaperone activity under cold stress conditions

Plant Cell & Environment ◽

10.1111/j.1365-3040.2009.02101.x ◽

2010 ◽

Cited By ~ 4

Author(s):

JOO Y. KIM ◽

WON Y. KIM ◽

KYUNG J. KWAK ◽

SEUNG H. OH ◽

YEON S. HAN ◽

...

Keyword(s):

Cold Stress ◽

Zinc Finger ◽

Rna Binding ◽

Binding Protein ◽

Rna Binding Protein ◽

Chaperone Activity ◽

Stress Conditions ◽

Rna Chaperone

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Cold-Inducible RNA-Binding Protein Prevents an Excessive Heart Rate Response to Stress by Targeting Phosphodiesterase

Circulation Research ◽

10.1161/circresaha.119.316322 ◽

2020 ◽

Vol 126 (12) ◽

pp. 1706-1720

Author(s):

Duanyang Xie ◽

Li Geng ◽

Ke Xiong ◽

Tingting Zhao ◽

Shuo Wang ◽

...

Keyword(s):

Heart Rate ◽

Stress Response ◽

Rna Binding ◽

Binding Protein ◽

Rna Binding Protein ◽

Stress Conditions ◽

Pde4 Inhibitor ◽

Mechanistic Study ◽

Heart Rate Regulation ◽

Posttranscriptional Level

Rationale: The stress response of heart rate, which is determined by the plasticity of the sinoatrial node (SAN), is essential for cardiac function and survival in mammals. As an RNA-binding protein, CIRP (cold-inducible RNA-binding protein) can act as a stress regulator. Previously, we have documented that CIRP regulates cardiac electrophysiology at posttranscriptional level, suggesting its role in SAN plasticity, especially upon stress conditions. Objective: Our aim was to clarify the role of CIRP in SAN plasticity and heart rate regulation under stress conditions. Methods and Results: Telemetric ECG monitoring demonstrated an excessive acceleration of heart rate under isoprenaline stimulation in conscious CIRP-KO (knockout) rats. Patch-clamp analysis and confocal microscopic Ca 2+ imaging of isolated SAN cells demonstrated that isoprenaline stimulation induced a faster spontaneous firing rate in CIRP-KO SAN cells than that in WT (wild type) SAN cells. A higher concentration of cAMP—the key mediator of pacemaker activity—was detected in CIRP-KO SAN tissues than in WT SAN tissues. RNA sequencing and quantitative real-time polymerase chain reaction analyses of single cells revealed that the 4B and 4D subtypes of PDE (phosphodiesterase), which controls cAMP degradation, were significantly decreased in CIRP-KO SAN cells. A PDE4 inhibitor (rolipram) abolished the difference in beating rate resulting from CIRP deficiency. The mechanistic study showed that CIRP stabilized the mRNA of Pde4b and Pde4d by direct mRNA binding, thereby regulating the protein expression of PDE4B and PDE4D at posttranscriptional level. Conclusions: CIRP acts as an mRNA stabilizer of specific PDEs to control the cAMP concentration in SAN, maintaining the appropriate heart rate stress response.

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