Abscisic acid-dependent multisite phosphorylation regulates the activity of a transcription activator AREB1 Export

@article{citeulike:2192282, abstract = {bZIP-type transcription factors AREBs/ABFs bind an abscisic acid (ABA)-responsive cis-acting element named ABRE and transactivate downstream gene expression in Arabidopsis. Because AREB1 overexpression could not induce downstream gene expression, activation of AREB1 requires ABA-dependent posttranscriptional modification. We confirmed that ABA activated 42-kDa kinase activity, which, in turn, phosphorylated Ser/Thr residues of R-X-X-S/T sites in the conserved regions of AREB1. Amino acid substitutions of R-X-X-S/T sites to Ala suppressed transactivation activity, and multiple substitution of these sites resulted in almost complete suppression of transactivation activity in transient assays. In contrast, substitution of the Ser/Thr residues to Asp resulted in high transactivation activity without exogenous ABA application. A phosphorylated, transcriptionally active form was achieved by substitution of Ser/Thr in all conserved R-X-X-S/T sites to Asp. Transgenic plants overexpressing the phosphorylated active form of AREB1 expressed many ABA-inducible genes, such as RD29B, without ABA treatment. These results indicate that the ABA-dependent multisite phosphorylation of AREB1 regulates its own activation in plants. 10.1073/pnas.0505667103}, author = {Furihata, Takashi and Maruyama, Kyonoshin and Fujita, Yasunari and Umezawa, Taishi and Yoshida, Riichiro and Shinozaki, Kazuo and Yamaguchi-Shinozaki, Kazuko}, citeulike-article-id = {2192282}, citeulike-linkout-0 = {http://dx.doi.org/10.1073/pnas.0505667103}, citeulike-linkout-1 = {http://www.pnas.org/cgi/content/abstract/103/6/1988}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/16446457}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=16446457}, day = {7}, doi = {10.1073/pnas.0505667103}, journal = {Proceedings of the National Academy of Sciences}, keywords = {aba, cold, stress, water}, month = {February}, number = {6}, pages = {1988--1993}, posted-at = {2008-01-03 20:56:54}, priority = {5}, title = {Abscisic acid-dependent multisite phosphorylation regulates the activity of a transcription activator AREB1}, url = {http://dx.doi.org/10.1073/pnas.0505667103}, volume = {103}, year = {2006} }

TY - JOUR ID - citeulike:2192282 L3 - citeulike-article-id:2192282 N2 - bZIP-type transcription factors AREBs/ABFs bind an abscisic acid (ABA)-responsive cis-acting element named ABRE and transactivate downstream gene expression in Arabidopsis. Because AREB1 overexpression could not induce downstream gene expression, activation of AREB1 requires ABA-dependent posttranscriptional modification. We confirmed that ABA activated 42-kDa kinase activity, which, in turn, phosphorylated Ser/Thr residues of R-X-X-S/T sites in the conserved regions of AREB1. Amino acid substitutions of R-X-X-S/T sites to Ala suppressed transactivation activity, and multiple substitution of these sites resulted in almost complete suppression of transactivation activity in transient assays. In contrast, substitution of the Ser/Thr residues to Asp resulted in high transactivation activity without exogenous ABA application. A phosphorylated, transcriptionally active form was achieved by substitution of Ser/Thr in all conserved R-X-X-S/T sites to Asp. Transgenic plants overexpressing the phosphorylated active form of AREB1 expressed many ABA-inducible genes, such as RD29B, without ABA treatment. These results indicate that the ABA-dependent multisite phosphorylation of AREB1 regulates its own activation in plants. 10.1073/pnas.0505667103 IS - 6 JF - Proceedings of the National Academy of Sciences EP - 1993 TI - Abscisic acid-dependent multisite phosphorylation regulates the activity of a transcription activator AREB1 VL - 103 SP - 1988 KW - aba KW - cold KW - stress KW - water AU - Furihata, Takashi AU - Maruyama, Kyonoshin AU - Fujita, Yasunari AU - Umezawa, Taishi AU - Yoshida, Riichiro AU - Shinozaki, Kazuo AU - Yamaguchi-Shinozaki, Kazuko PY - 2006/02/07/ UR - http://dx.doi.org/10.1073/pnas.0505667103 ER -