UPL5 modulates WHY2 protein distribution in a Kub-site dependent ubiquitination in response to [Ca2+]cyt-induced leaf senescence

Wei Lan; Weibo Ma; Shuai Zheng; Ping Yang; Yuhao Qiu; Wenfang Lin; Yujun Ren; Ying Miao

doi:10.1016/j.isci.2023.106216

UPL5 modulates WHY2 protein distribution in a Kub-site dependent ubiquitination in response to [Ca²⁺]_cyt-induced leaf senescence

iScience. 2023 Mar 6;26(3):106216. doi: 10.1016/j.isci.2023.106216. eCollection 2023 Mar 17.

Authors

Wei Lan¹, Weibo Ma¹, Shuai Zheng¹, Ping Yang¹, Yuhao Qiu¹, Wenfang Lin¹, Yujun Ren¹, Ying Miao¹

Affiliation

¹ Fujian Provincial Key Laboratory of Plant Functional Biology, College of Life Sciences, Fujian Agriculture and Forestry University, Fuzhou 350002, China.

Abstract

The translocation of proteins between various compartments of cells is the simplest and most direct way of an/retrograde communication. However, the mechanism of protein trafficking is far understood. In this study, we showed that the alteration of WHY2 protein abundance in various compartments of cells was dependent on a HECT-type ubiquitin E3 ligase UPL5 interacting with WHY2 in the cytoplasm, plastid, and nucleus, as well as mitochondrion to selectively ubiquitinate various Kub-sites (Kub 45 and Kub 227) of WHY2. Plastid genome stability can be maintained by the UPL5-WHY2 module, accompany by the alteration of photosystem activity and senescence-associated gene expression. In addition, the specificity of UPL5 ubiquitinating various Kub-sites of WHY2 was responded to cold or CaCl₂ stress, in a dose [Ca²⁺]_cyt-dependent manner. This demonstrates the integration of the UPL5 ubiquitination with the regulation of WHY2 distribution and retrograde communication between organelle and nuclear events of leaf senescence.

Keywords: Biological sciences; Natural sciences; Plant Biology; Plant biology.

Publication types

Retracted Publication