| Name | 26S proteasome (protein family or complex) |
|---|---|
| Synonyms | 26 proteasome; 26S Proteasome; 26S protease; 26S proteases |
| Name | gibberellins |
|---|---|
| CAS | gibberellins |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 12969426 | Downes BP, Stupar RM, Gingerich DJ, Vierstra RD: The HECT ubiquitin-protein ligase (UPL) family in Arabidopsis: UPL3 has a specific role in trichome development. Plant J. 2003 Sep;35(6):729-42. Attachment of one or more ubiquitins (Ubs) to various intracellular proteins has a number of roles in plants including the selective removal of regulatory proteins by the 26S proteasome. The upl3 trichomes also often undergo an additional round of endoreplication resulting in enlarged nuclei with ploidy levels of up to 64C. upl3 plants are hypersensitive to -3 consistent with the role of gibberellins in trichome development. |
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| 16740147 | Oh E, Yamaguchi S, Kamiya Y, Bae G, Chung WI, Choi G: Light activates the degradation of PIL5 protein to promote seed germination through in Arabidopsis. Plant J. 2006 Jul;47(1):124-39. Epub 2006 Jun 1. Lastly, we showed that red and far-red light signals trigger PIL5 protein degradation through the 26S proteasome, thus releasing the inhibition of bioactive GA biosynthesis by PIL5. |
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| 18703407 | Itoh H, Ueguchi-Tanaka M, Matsuoka M: Molecular biology of gibberellins signaling in higher plants. Int Rev Cell Mol Biol. 2008;268:191-221. These results suggest that formation of a GID1-GA-DELLA protein complex targets DELLA protein into the ubiquitin-26S proteasome pathway for degradation. |
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| 17900970 | Jiang C, Fu X: GA action: turning on de-DELLA repressing signaling. Curr Opin Plant Biol. 2007 Oct;10(5):461-5. Epub 2007 Sep 27. Phytohormone gibberellins (GA) are a large family of tetracyclic diterpenoids and play the important roles in modulation of plant growth and development throughout the plant life cycle. GA depresses its signaling by the GA-promoted destabilization of the DELLA protein growth repressors via 26S proteasome pathway. |
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| 17627823 | Yasumura Y, Crumpton-Taylor M, Fuentes S, Harberd NP: Step-by-step acquisition of the -DELLA growth-regulatory mechanism during land-plant evolution. Curr Biol. 2007 Jul 17;17(14):1225-30. Subsequent 26S proteasome-mediated destruction of the DELLAs promotes growth [13-17]. |
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| 15155881 | Dill A, Thomas SG, Hu J, Steber CM, Sun TP: The Arabidopsis F-box protein SLEEPY1 targets signaling repressors for -induced degradation. Plant Cell. 2004 Jun;16(6):1392-405. Epub 2004 May 21. These findings suggested that SLY1 recruits RGA to the SCFSLY1 E3 ligase complex for ubiquitination and subsequent degradation by the 26S proteasome. |
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| 18713393 | Gao XH, Huang XZ, Xiao SL, Fu XD: Evolutionarily conserved DELLA-mediated signaling in plants. J Integr Plant Biol. 2008 Jul;50(7):825-34. Gibberellins (GAs) play important roles in many essential plant growth and development processes. GA perception is mediated by GID1, and the key event of GA signaling is the degradation of DELLA proteins via the 26S proteasome pathway. |
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| 12724538 | McGinnis KM, Thomas SG, Soule JD, Strader LC, Zale JM, Sun TP, Steber CM: The Arabidopsis SLEEPY1 gene encodes a putative F-box subunit of an SCF E3 ubiquitin ligase. Plant Cell. 2003 May;15(5):1120-30. This result suggests SCF (SLY1)-targeted degradation of RGA through the 26S proteasome pathway. |
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| 11828019 | Lorenzo O, Nicolas C, Nicolas G, Rodriguez D: GA (3)-induced expression of a new functional AAA-ATPase (FsA1) is correlated with the onset of germination in Fagus sylvatica L. seeds (beechnuts). Plant Cell Physiol. 2002 Jan;43(1):27-34. This clone shows high identity with members of the AAA superfamily, for ATPases Associated with a variety of cellular Activities, encoding subunit 8 of the 26S proteasome or Tat binding proteins (TBPs). |
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| 18930434 | Schwechheimer C, Willige BC: Shedding light on signalling. Curr Opin Plant Biol. 2009 Feb;12(1):57-62. Epub 2008 Oct 17. Their presence or their GA-dependent turnover via the 26S proteasome correlates to a large extent with the repression or derepression, respectively, of GA-dependent growth responses. |
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| 14557046 | Itoh H, Matsuoka M, Steber CM: A role for the ubiquitin-26S-proteasome pathway in signaling. Trends Plant Sci. 2003 Oct;8(10):492-7. |
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| 15377219 | Sun TP, Gubler F: Molecular mechanism of signaling in plants. Annu Rev Plant Biol. 2004;55:197-223. Recent evidence indicates that the DELLA proteins are targeted for degradation by an E3 ubiquitin ligase SCF complex through the ubiquitin-26S proteasome pathway. |
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| 16492475 | Thomas SG, Rieu I, Steber CM: metabolism and signaling. Vitam Horm. 2005;72:289-338. Gibberellins (GAs) are a family of plant hormones controlling many aspects of plant growth and development including stem elongation, germination, and the transition from vegetative growth to flowering. |
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| 16209355 | Kowalczyk S, Hadowska E, Piekarska A: [Plant ubiquitylation and proteolytic systems, the key elements in hormonal signaling pathways]. Postepy Biochem. 2005;51(2):171-87. In Arabidopsis thaliana more than 1300 genes (approximately 5% of the proteome) encode components of the ubiquitin/26S proteasome pathway. The role of the SCF is to ubiquitylate repressors of hormone response (auxin, gibberellins), whereas in response to ethylene, abscisic acid and brassinosteroids the SCF participate in degradation of positive regulators in the absence of the hormone. |
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| 15161962 | Fu X, Richards DE, Fleck B, Xie D, Burton N, Harberd NP: The Arabidopsis mutant sleepy1gar2-1 protein promotes plant growth by increasing the affinity of the SCFSLY1 E3 ubiquitin ligase for DELLA protein substrates. Plant Cell. 2004 Jun;16(6):1406-18. Epub 2004 May 25. stimulates growth via 26S proteasome-dependent destruction of DELLAs, thus relieving DELLA-mediated growth restraint. |
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| 15491916 | Schwechheimer C, Calderon Villalobos LI: Cullin-containing E3 ubiquitin ligases in plant development. Curr Opin Plant Biol. 2004 Dec;7(6):677-86. E3 ubiquitin ligases specifically bind degradation substrates and mediate their poly-ubiquitylation, a prerequisite for their degradation by the 26S proteasome. |
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