2011
DOI: 10.1104/pp.111.180893
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The SINA E3 Ligase OsDIS1 Negatively Regulates Drought Response in Rice      

Abstract: Ubiquitin-regulated protein degradation is a critical regulatory mechanism that controls a wide range of biological processes in plants. Here, we report that OsDIS1 (for Oryza sativa drought-induced SINA protein 1), a C3HC4 RING finger E3 ligase, is involved in drought-stress signal transduction in rice (O. sativa). The expression of OsDIS1 was up-regulated by drought treatment. In vitro ubiquitination assays showed that OsDIS1 possessed E3 ubiquitin ligase activity and that the conserved region of the RING fi… Show more

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Cited by 164 publications
(103 citation statements)
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“…This might have been due to the interaction between SDIR1 and SDIRIP1 quickly driving SDIRIP1 degradation via the 26S proteasome. Similarly, Ning et al (2011) described that the colocalization of the rice (Oryza sativa) RING finger E3 ligase OsDIS1 (DROUGHT-INDUCED SEVEN IN ABSENTIA PROTEIN1) with its substrate Os-Nek6 (NEVER-IN-MITOSIS/ ASPERGILLUS-RELATED KINASE6) was almost undetectable in vivo, but Os-DIS1 H71Y , losing E3 activity due to a point mutation in the RING motif, was well colocalized with Os-Nek6. SDIR1 H234Y , which destroyed the E3 activity of SDIR1 but remained in the same cellular localization as SDIR1, could still interact with SDIRIP1 in yeast two-hybrid assays.…”
Section: Sdirip1-sdir1 Interaction In Vivomentioning
confidence: 92%
“…This might have been due to the interaction between SDIR1 and SDIRIP1 quickly driving SDIRIP1 degradation via the 26S proteasome. Similarly, Ning et al (2011) described that the colocalization of the rice (Oryza sativa) RING finger E3 ligase OsDIS1 (DROUGHT-INDUCED SEVEN IN ABSENTIA PROTEIN1) with its substrate Os-Nek6 (NEVER-IN-MITOSIS/ ASPERGILLUS-RELATED KINASE6) was almost undetectable in vivo, but Os-DIS1 H71Y , losing E3 activity due to a point mutation in the RING motif, was well colocalized with Os-Nek6. SDIR1 H234Y , which destroyed the E3 activity of SDIR1 but remained in the same cellular localization as SDIR1, could still interact with SDIRIP1 in yeast two-hybrid assays.…”
Section: Sdirip1-sdir1 Interaction In Vivomentioning
confidence: 92%
“…Hot pepper (Capsicum annuum) RING MEMBRANE-ANCHOR 1 HOMOLOG1 functions as an E3 ligase, ubiquitinating the plasma membrane aquaporin PIP2;1 under water-deficient conditions ). The C3HC4 RING finger E3 ligase OsDIS1, which is predominantly localized in the nucleus, plays a negative role in drought stress tolerance through the transcriptional regulation of diverse stress-related genes and possibly through the posttranslational regulation of OsNek6 in rice (Ning et al, 2011). The rice RING finger E3 ligase HEAT AND COLD INDUCED1 drives the nuclear export of multiple substrate proteins, and its heterogenous overexpression enhances acquired thermotolerance (Lim et al, 2013a).…”
mentioning
confidence: 99%
“…The nek6 mutation enhanced stress tolerance whereas NEK6 overexpression reduced stress tolerance in the study by Lee et al (2010). In that by Zhang et al (2011), the nek6-1 mutation led to reduced stress tolerance whereas NEK6 overexpression promoted stress tolerance. Although the reason for this discrepancy remains unknown, it could be due to differences in the growth conditions, stress treatments, and the nek6 alleles used in two studies.…”
Section: Involvement Of Plant Neks In Stress Responsesmentioning
confidence: 98%