Dataset Information

Comprehensive proteomics and phosphorylation analysis revealed the negative role of VaVIP1 in cold tolerance of grapevine.

ABSTRACT: Grapevine, a globally important fruit crop. Low temperature limits grapevine yield, quality and geographical distribution. Protein post-translational modification is involved in cold tolerance of grapevine. In order to cultivate new varieties of grapevine cold tolerance, we conducted an integrated proteomic and phosphoproteomic analysis of Vitis amurensis, identifying widespread changes involving 4,797 proteins, 10,104 phosphorylation sites and 56 motif sequences. Cold treatment resulted in 165 differential phosphorylation proteins and 635 differential phosphorylation sites. GO enrichment showed that differential phosphorylation proteins were mainly concentrated in biological processes, cellular components and molecular functions. Functional enrichment highlighted critical roles for metabolic and signaling pathways, including phenylpropanoid biosynthesis and MAPK cascades. From this dataset, we focused on the bZIP transcription factor VaVIP1 and uncovered its negative regulatory role in cold tolerance. VaVIP1 overexpression can make the grapevine damage more severe, as evidenced by increased oxidative stress, membrane damage, and attenuated osmotic adjustment. On the molecular mechanism, VaVIP1 overexpression suppressed the cold-induced activation of key genes in the CBF-regulatory pathway. Our work not only expands the phosphoproteomic resource for plants but also delineates a novel mechanism where VaVIP1 acts as a negative regulator to cold tolerance, providing a valuable theoretical foundation for improving cold tolerance in grapevine.

ORGANISM(S): Vitis Vinifera

SUBMITTER: Xiuming Zhang

PROVIDER: PXD072186 | iProX | Thu Dec 18 00:00:00 GMT 2025

REPOSITORIES: iProX

ACCESS DATA

Similar Datasets

Project description:Cold-sensitive Cavendish Banana and relatively cold-tolerant Dajiao (Musa spp.) comprise an important part of diets for millions of people around the globe. Low temperature is one of the key environment stresses which greatly affect the global banana production. However, little is known about the changes of global protein phosphorylation in Musa spp. and their regulatory roles in response to cold stress. In this study, we employed a TMT6-plex quantitative analysis to conduct a global phosphoproteome profiling between Cavendish Banana and Dajiao subject to the cold stress for 0 hour and 3 hour. A total of 679 phosphopeptides containing 772 distinct phosphorylated sites from 529 phosphoproteins were identified in Cavendish Banana, 180 phosphorylation sites (belonging to 147 phosphoproteins) were differentially changed after 3 h cold stress. While in Dajiao 241 phosphopeptides with 271 individual phosphosites from 207 phosphoproteins were confidently identified, and 83 phosphorylation sites from 63 phosphoproteins were differentially changed under 3 h cold stress. Bioinformatic analysis of protein interaction network indicated that Mitogen-activated protein kinase kinase 2 (MKK2) was located in the center of the MAPK signaling network along with 7 other members whose phosphorylated site abundances were remarkably differentiated between Cavendish Banana and Dajiao in response to cold stress. Western blotting of MKK2 protein and its T31 phosphorylated site showed the increased expression of MKK2 in the time course of cold stress, with no detectable T31 phosphorylation in Cavendish Banana. On the contrary, the decreased MKK2 expression with increased T31 phosphorylation was consistently observed in Dajiao. These results suggest that the MKK2 interaction network in Dajiao, along with other cold-specific phosphoproteins found in this study, appears to play an important role in the molecular mechanisms of Dajiao being high tolerance to cold stress. The results also provide new evidence that cellular MKK2 phosphorylation as a signaling pathway plays an important role in abiotic stress tolerance that serves as a universal plant cold tolerance mechanism. To the best of our knowledge, this is the first report of MKK2 network involved in the regulatory of the Musa spp. response to cold stress.

Project description:Minichromosome maintenance protein 2 (MCM2) is a licensing factor for DNA replication. It interacts with other MCM proteins to comprise MCM2-7 complex, which acts as a helicase for DNA unwinding and limits DNA replication to one round per cell cycle. MCM2 has been widely used as a biomarker for proliferation in many types of cancer. However, the molecular regulation underlying MCM2 in lung cancer cells is poorly understood. In this study, we investigated the role of MCM2 in lung adenocarcinoma A549 (wild-type p53) and H1299 (null p53) cells. MCM2 overexpression increased cell proliferation in A549 cells while silencing MCM2 decreased cell proliferation in H1299 cells. We performed global quantitative phosphoproteomic analysis to uncover the important downstream networks regulated by MCM2 in lung cancer cells. We identified 1484 phosphorylation sites in 593 phosphoproteins of MCM2-overexpressed A549 cells. Of these phosphosites, 110 phosphoproteins were significantly changed in response to MCM2 overexpression. In addition, we identified 1599 phosphorylation sites in 592 phosphoproteins of MCM2-silenced H1299 cells. Of these phosphosites, 57 phosphoproteins were significantly changed in response to MCM2 silencing. The differentially regulated phosphoproteins are involved in biological functions such as RNA splicing, cell cycle and cytoskeleton regulation. Functional study demonstrated that MCM2 overexpression promoted cell migration in A549 cells. Moreover, silencing MCM2 inhibits cell migration and induces cell cycle arrest in H1299 cells. Furthermore, we observed a common phosphorylation change at Ser-99 of high mobility group protein HMG-I/HMG-Y (HMGA1) in both MCM2 overexpression and silencing, indicating an important regulatory effect of Ser-99 HMGA1 on lung cancer cells. The phosphoproteomic profiling of MCM2 in lung cancer cells provides new insight about phosphorylation networks regulated by MCM2 and reveals novel targets for lung cancer therapy.

Dataset Information

Comprehensive proteomics and phosphorylation analysis revealed the negative role of VaVIP1 in cold tolerance of grapevine.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets