Protein post-translational modifications in auxin signaling

Cui, Xiankui; Wang, Junxia; Li, Ké; Lv, Bingsheng; Hou, Bing-Kai; Ding, Zhaojun

doi:10.1016/j.jgg.2023.07.002

Cited by 9 publications

(2 citation statements)

References 143 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Because phosphorylation frequently regulates the stability of target protein (Cui et al, 2024; Jiang et al, 2019), we hypothesized that CARKs may enhance the stability of D6PK through phosphorylation. To test this notion, an in vitro cell‐free degradation assay was performed.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Cytosolic ABA Receptor Kinases phosphorylate the D6 PROTEIN KINASE leading to its stabilization which promotes Arabidopsis growth

He,

Li,

et al. 2024

Plant Cell & Environment

View full text Add to dashboard Cite

The polar auxin transport is required for proper plant growth and development. D6 PROTEIN KINASE (D6PK) is required for the phosphorylation of PIN‐FORMED (PIN) auxin efflux carriers to regulate auxin transport, while the regulation of D6PK stabilization is still poorly understood. Here, we found that Cytosolic ABA Receptor Kinases (CARKs) redundantly interact with D6PK, and the interactions are dependent on CARKs' kinase activities. Similarly, CARK3 also could interact with paralogs of D6PK, including D6PKL1, D6PKL2, and D6PKL3. The genetic analysis shows that D6PK acts the downstream of CARKs to regulate Arabidopsis growth, including hypocotyl, leaf area, vein formation, and the length of silique. Loss‐of‐function of CARK3 in overexpressing GFP‐D6PK plants leads to reduce the level of D6PK protein, thereby rescues plant growth. In addition, the cell‐free degradation assays indicate that D6PK is degraded through 26 S proteasome pathway, while the phosphorylation by CARK3 represses this process in cells. In summary, D6PK stabilization by the CARK family is required for auxin‐mediated plant growth and development.

show abstract

Section: Resultsmentioning

confidence: 99%

“…The abundance of protein is determined by the balance of protein synthesis and protein degradation. Ubiquitination modification is involved in auxin signaling by regulating protein abundance (Cui et al, 2024; Santner & Estelle, 2010). The efficiency and rate of ubiquitination can be affected by phosphorylation (Sarid‐Krebs et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

Cytosolic ABA Receptor Kinases phosphorylate the D6 PROTEIN KINASE leading to its stabilization which promotes Arabidopsis growth

He,

Li,

et al. 2024

Plant Cell & Environment

View full text Add to dashboard Cite

show abstract

VIK‐Mediated Auxin Signaling Regulates Lateral Root Development in Arabidopsis

Shang,

Wei,

et al. 2024

Advanced Science

View full text Add to dashboard Cite

The crucial role of TIR1‐receptor‐mediated gene transcription regulation in auxin signaling has long been established. In recent years, the significant role of protein phosphorylation modifications in auxin signal transduction has gradually emerged. To further elucidate the significant role of protein phosphorylation modifications in auxin signaling, a phosphoproteomic analysis in conjunction with auxin treatment has identified an auxin activated Mitogen‐activated Protein Kinase Kinase Kinase (MAPKKK) VH1‐INTERACTING Kinase (VIK), which plays an important role in auxin‐induced lateral root (LR) development. In the vik mutant, auxin‐induced LR development is significantly attenuated. Further investigations show that VIK interacts separately with the positive regulator of LR development, LATERAL ORGAN BOUNDARIES‐DOMAIN18 (LBD18), and the negative regulator of LR emergence, Ethylene Responsive Factor 13 (ERF13). VIK directly phosphorylates and stabilizes the positive transcription factor LBD18 in LR formation. In the meantime, VIK directly phosphorylates the negative regulator ERF13 at Ser168 and Ser172 sites, causing its degradation and releasing the repression by ERF13 on LR emergence. In summary, VIK‐mediated auxin signaling regulates LR development by enhancing the protein stability of LBD18 and inducing the degradation of ERF13, respectively.

show abstract