Molecular dissection of <i>Oryza sativa salt‐induced <scp>RING</scp> Finger Protein 1</i> (<i><scp>OsSIRP1</scp></i>): possible involvement in the sensitivity response to salinity stress

Hwang, Sun‐Goo; Kim, Jung Ju; Lim, Sung Don; Park, Yong Chan; Moon, Jun-Cheol; Jang, Cheol Seong

doi:10.1111/ppl.12459

Cited by 39 publications

(18 citation statements)

References 42 publications

(53 reference statements)

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“…STRF1 mainly regulates the expression of membrane transport-related proteins. OsSIRP1 is a negative regulator of salt tolerance, and its target protein needs to be further studied [49,60]. The microtubule-associated RING finger protein 1 (OsMAR1), an E3 ligase, acts as a negative regulator for salt-stress response through the regulation of the O. sativa chymotrypsin protease inhibitor 2 (OsCPI2), but anther rice RING H2-type E3 ligase, OsSIRH2-14 (previously named OsRFPH2-14), plays a positive role in salinity tolerance by regulating salt-related proteins, including an HKT-type Na+ transporter (OsHKT2; 1) [55,59].…”

Section: Ring-finger Proteins Are Involved In Salt and Aluminium Resimentioning

confidence: 99%

Research Progress on Plant RING-Finger Proteins

Sun

Ahmed

et al. 2019

Genes

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E3 ubiquitin ligases are the most expanded components of the ubiquitin proteasome system (UPS). They mediate the recognition of substrates and later transfer the ubiquitin (Ub) of the system. Really Interesting New Gene (RING) finger proteins characterized by the RING domain, which contains 40–60 residues, are thought to be E3 ubiquitin ligase. RING-finger proteins play significant roles in plant growth, stress resistance, and signal transduction. In this study, we mainly describe the structural characteristics, classifications, and subcellular localizations of RING-finger proteins, as well the physiological processes of RING-finger proteins in plant growth and development. We also summarize the functions of plant RING-finger proteins in plant stress resistance. Finally, further research on plant RING-finger proteins is suggested, thereby establishing a strong foundation for the future study of plant RING-finger proteins.

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Section: Ring-finger Proteins Are Involved In Salt and Aluminium Resimentioning

confidence: 99%

Research Progress on Plant RING-Finger Proteins

Sun

Ahmed

et al. 2019

Genes

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“…The drought-induced AtERF53 could be degraded by RING E3 Ligase RGLG1 and RGLG2 that acts as negative regulators in drought tolerance [ 53 ]. Overexpression of salt-induced RING E3 ligase OsSIRP1 reduced salt tolerance in Arabidopsis [ 54 ]. In addition, several substrate receptors of CUL4 E3 ligases, DWAs, regulate ABA responses negatively [ 55 , 56 ].…”

Section: Introductionmentioning

confidence: 99%

PARAQUAT TOLERANCE3 Is an E3 Ligase That Switches off Activated Oxidative Response by Targeting Histone-Modifying PROTEIN METHYLTRANSFERASE4b

Luo

Cai

et al. 2016

PLoS Genet

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Oxidative stress is unavoidable for aerobic organisms. When abiotic and biotic stresses are encountered, oxidative damage could occur in cells. To avoid this damage, defense mechanisms must be timely and efficiently modulated. While the response to oxidative stress has been extensively studied in plants, little is known about how the activated response is switched off when oxidative stress is diminished. By studying Arabidopsis mutant paraquat tolerance3, we identified the genetic locus PARAQUAT TOLERANCE3 (PQT3) as a major negative regulator of oxidative stress tolerance. PQT3, encoding an E3 ubiquitin ligase, is rapidly down-regulated by oxidative stress. PQT3 has E3 ubiquitin ligase activity in ubiquitination assay. Subsequently, we identified PRMT4b as a PQT3-interacting protein. By histone methylation, PRMT4b upregulates the expression of APX1 and GPX1, encoding two key enzymes against oxidative stress. On the other hand, PRMT4b is recognized by PQT3 for targeted degradation via 26S proteasome. Therefore, we have identified PQT3 as an E3 ligase that acts as a negative regulator of activated response to oxidative stress and found that histone modification by PRMT4b at APX1 and GPX1 loci plays an important role in oxidative stress tolerance.

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“…The ectopic overexpression of OsSIRP1 in Arabidopsis reduces tolerance for salinity stress during seed germination and root growth. Thus, it has been elucidated OsSIRP1 may act as a negative regulator of salinity stress tolerance ( 48 ).…”

Section: Introductionmentioning

confidence: 99%

RING E3 ligases: key regulatory elements are involved in abiotic stress responses in plants

et al. 2017

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Plants are constantly exposed to a variety of abiotic stresses, such as drought, heat, cold, flood, and salinity. To survive under such unfavorable conditions, plants have evolutionarily developed their own resistant-mechanisms. For several decades, many studies have clarified specific stress response pathways of plants through various molecular and genetic studies. In particular, it was recently discovered that ubiquitin proteasome system (UPS), a regulatory mechanism for protein turn over, is greatly involved in the stress responsive pathways. In the UPS, many E3 ligases play key roles in recognizing and tethering poly-ubiquitins on target proteins for subsequent degradation by the 26S proteasome. Here we discuss the roles of RING ligases that have been defined in related to abiotic stress responses in plants.

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Molecular dissection of Oryza sativa salt‐induced RING Finger Protein 1 (OsSIRP1): possible involvement in the sensitivity response to salinity stress

Cited by 39 publications

References 42 publications

Research Progress on Plant RING-Finger Proteins

Research Progress on Plant RING-Finger Proteins

PARAQUAT TOLERANCE3 Is an E3 Ligase That Switches off Activated Oxidative Response by Targeting Histone-Modifying PROTEIN METHYLTRANSFERASE4b

RING E3 ligases: key regulatory elements are involved in abiotic stress responses in plants

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