The role of HEXOKINASE1 in Arabidopsis leaf growth

生物 突变体 细胞生长 拟南芥 叶绿体 生物化学 蔗糖 细胞生物学 基因
作者
Judith Van Dingenen,Mattias Vermeersch,Liesbeth De Milde,Sander Hulsmans,Nancy De Winne,Jelle Van Leene,Nathalie González,Stijn Dhondt,Geert De Jaeger,Filip Rolland,Dirk Inzé
出处
期刊:Plant Molecular Biology [Springer Science+Business Media]
卷期号:99 (1-2): 79-93 被引量:27
标识
DOI:10.1007/s11103-018-0803-0
摘要

Here, we used a hxk1 mutant in the Col-0 background. We demonstrated that HXK1 regulates cell proliferation and expansion early during leaf development, and that HXK1 is involved in sucrose-induced leaf growth stimulation independent of GPT2. Furthermore, we identified KINγ as a novel HXK1-interacting protein. In the last decade, extensive efforts have been made to unravel the underlying mechanisms of plant growth control through sugar availability. Signaling by the conserved glucose sensor HEXOKINASE1 (HXK1) has been shown to exert both growth-promoting and growth-inhibitory effects depending on the sugar levels, the environmental conditions and the plant species. Here, we used a hxk1 mutant in the Col-0 background to investigate the role of HXK1 during leaf growth in more detail and show that it is affected in both cell proliferation and cell expansion early during leaf development. Furthermore, the hxk1 mutant is less sensitive to sucrose-induced cell proliferation with no significant increase in final leaf growth after transfer to sucrose. Early during leaf development, transfer to sucrose stimulates expression of GLUCOSE-6-PHOSPHATE/PHOSPHATE TRANSPORTER2 (GPT2) and represses chloroplast differentiation. However, in the hxk1 mutant GPT2 expression was still upregulated by transfer to sucrose although chloroplast differentiation was not affected, suggesting that GPT2 is not involved in HXK1-dependent regulation of leaf growth. Finally, using tandem affinity purification of protein complexes from cell cultures, we identified KINγ, a protein containing four cystathionine β-synthase domains, as an interacting protein of HXK1.
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