TYPE-ONE PROTEIN PHOSPHATASE4 Regulates Pavement Cell Interdigitation by Modulating PIN-FORMED1 Polarity and Trafficking in Arabidopsis

Author:

Guo Xiaola1,Qin Qianqian1,Yan Jia1,Niu Yali1,Huang Bingyao1,Guan Liping1,Li Yuan2,Ren Dongtao2,Li Jia1,Hou Suiwen1

Affiliation:

1. Ministry of Education Key Laboratory of Cell Activities and Stress Adaptations, School of Life Sciences, Lanzhou University, Lanzhou 730000, China (X.G., Q.Q., J.Y., Y.N., B.H., L.G., J.L., S.H.); and

2. State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University, Beijing 100193, China (Y.L., D.R.)

Abstract

Abstract In plants, cell morphogenesis is dependent on intercellular auxin accumulation. The polar subcellular localization of the PIN-FORMED (PIN) protein is crucial for this process. Previous studies have shown that the protein kinase PINOID (PID) and protein phosphatase6-type phosphatase holoenzyme regulate the phosphorylation status of PIN1 in root tips and shoot apices. Here, we show that a type-one protein phosphatase, TOPP4, is essential for the formation of interdigitated pavement cell (PC) pattern in Arabidopsis (Arabidopsis thaliana) leaf. The dominant-negative mutant topp4-1 showed severely inhibited interdigitated PC growth. Expression of topp4-1 gene in wild-type plants recapitulated the PC defects in the mutant. Genetic analyses suggested that TOPP4 and PIN1 likely function in the same pathway to regulate PC morphogenesis. Furthermore, colocalization, in vitro and in vivo protein interaction studies, and dephosphorylation assays revealed that TOPP4 mediated PIN1 polar localization and endocytic trafficking in PCs by acting antagonistically with PID to modulate the phosphorylation status of PIN1. In addition, TOPP4 affects the cytoskeleton pattern through the Rho of Plant GTPase-dependent auxin-signaling pathway. Therefore, we conclude that TOPP4-regulated PIN1 polar targeting through direct dephosphorylation is crucial for PC morphogenesis in the Arabidopsis leaf.

Publisher

Oxford University Press (OUP)

Subject

Plant Science,Genetics,Physiology

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