Unknown

Dataset Information

0

SHAGGY-like kinase 12 regulates flowering through mediating CONSTANS stability in Arabidopsis.


ABSTRACT: Photoperiod is a major environmental cue that determines the floral transition from vegetative to reproductive development in flowering plants. Arabidopsis thaliana responds to photoperiodic signals mainly through a central regulator CONSTANS (CO). Although it has been suggested that phosphorylation of CO contributes to its role in photoperiodic control of flowering, how this is regulated so far remains unknown. Here, we report that a glycogen synthase kinase-3 member, SHAGGY-like kinase 12 (SK12), plays an important role in preventing precocious flowering through phosphorylating CO. Loss of function of SK12 causes early flowering. SK12 expression in seedlings is decreased during the floral transition, and its expression in vascular tissues is required for repressing flowering. SK12 interacts with and phosphorylates CO at threonine 119, thus facilitating CO degradation. Our findings suggest that site-specific phosphorylation of CO by SK12 is critical for modulating the photoperiodic output for the floral induction in Arabidopsis.

SUBMITTER: Chen Y 

PROVIDER: S-EPMC7292628 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature

altmetric image

Publications

SHAGGY-like kinase 12 regulates flowering through mediating CONSTANS stability in <i>Arabidopsis</i>.

Chen Ying Y   Song Shiyong S   Gan Yinbo Y   Jiang Lixi L   Yu Hao H   Shen Lisha L  

Science advances 20200612 24


Photoperiod is a major environmental cue that determines the floral transition from vegetative to reproductive development in flowering plants. <i>Arabidopsis thaliana</i> responds to photoperiodic signals mainly through a central regulator CONSTANS (CO). Although it has been suggested that phosphorylation of CO contributes to its role in photoperiodic control of flowering, how this is regulated so far remains unknown. Here, we report that a glycogen synthase kinase-3 member, SHAGGY-like kinase  ...[more]

Similar Datasets

| S-EPMC5224386 | biostudies-literature
| S-EPMC6966814 | biostudies-literature
| S-EPMC3295255 | biostudies-literature
| S-EPMC4267339 | biostudies-literature
| S-EPMC5854132 | biostudies-literature
| S-EPMC3997802 | biostudies-literature
| S-EPMC3816489 | biostudies-literature
| S-EPMC7575571 | biostudies-literature
| S-EPMC5495492 | biostudies-literature
| S-EPMC4887344 | biostudies-literature