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The Putative O-Linked N-Acetylglucosamine Transferase SPINDLY Inhibits Class I TCP Proteolysis to Promote Sensitivity to Cytokinin
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SYSNO ASEP 0463547 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title The Putative O-Linked N-Acetylglucosamine Transferase SPINDLY Inhibits Class I TCP Proteolysis to Promote Sensitivity to Cytokinin Author(s) Steiner, E. (IL)
Livne, S. (IL)
Kobinson-Katz, T. (IL)
Tal, L. (IL)
Pri-Tal, O. (IL)
Mosquna, A. (IL)
Tarkowská, Danuše (UEB-Q) RID, ORCID
Mueller, B. (DE)
Tarkowski, P. (CZ)
Weiss, D. (IL)Source Title Plant Physiology. - : Oxford University Press - ISSN 0032-0889
Roč. 171, č. 2 (2016), s. 1485-1494Number of pages 10 s. Language eng - English Country US - United States Keywords B RESPONSE REGULATORS ; ARABIDOPSIS-THALIANA ; SIGNAL-TRANSDUCTION Subject RIV EB - Genetics ; Molecular Biology R&D Projects LO1204 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Institutional support UEB-Q - RVO:61389030 UT WOS 000380699200055 DOI 10.1104/pp.16.00343 Annotation Arabidopsis (Arabidopsis thaliana) SPINDLY (SPY) is a putative serine and threonine O-linked N-acetylglucosamine transferase (OGT). While SPY has been shown to suppress gibberellin signaling and to promote cytokinin (CK) responses, its catalytic OGT activity was never demonstrated and its effect on protein fate is not known. We previously showed that SPY interacts physically and functionally with TCP14 and TCP15 to promote CK responses. Here, we aimed to identify how SPY regulates TCP14/15 activities and how these TCPs promote CK responses. We show that SPY activity is required for TCP14 stability. Mutation in the putative OGT domain of SPY (spy-3) stimulated TCP14 proteolysis by the 26S proteasome, which was reversed by mutation in CULLIN1 (CUL1), suggesting a role for SKP, CUL1, F-box E3 ubiquitin ligase in TCP14 proteolysis. TCP14 proteolysis in spy-3 suppressed all TCP14 misexpression phenotypes, including the enhanced CK responses. The increased CK activity in TCP14/15-overexpressing flowers resulted from increased sensitivity to the hormone and not from higher CK levels. TCP15 overexpression enhanced the response of the CK-induced synthetic promoter pTCS to CK, suggesting that TCP14/15 affect early steps in CK signaling. We propose that posttranslational modification of TCP14/15 by SPY inhibits their proteolysis and that the accumulated proteins promote the activity of the CK phosphorelay cascade in developing Arabidopsis leaves and flowers. Workplace Institute of Experimental Botany Contact David Klier, knihovna@ueb.cas.cz, Tel.: 220 390 469 Year of Publishing 2017
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