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Identifying the proteome and phosphoproteome regulated by the Mck1 kinase in response to glucose starvation

ABSTRACT: Using the 11-plex TMT labelling kit, the project intended to identify the proteins and phosphoproteins in the S. cerevisiae proteome that are differentially regulated by the Mck1 kinase during the transition from exponential growth to the post-diauxic shift phase.

INSTRUMENT(S):

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Nianshu Zhang

LAB HEAD: Nianshu Zhang

PROVIDER: PXD055585 | Pride | 2025-05-26

REPOSITORIES: Pride

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			Action	DRS
	20200722_HZ_SC_TMT11plex_Phos_highpHRP_F01.raw	Raw
	20200722_HZ_SC_TMT11plex_Phos_highpHRP_F02.raw	Raw
	20200722_HZ_SC_TMT11plex_Phos_highpHRP_F03.raw	Raw
	20200722_HZ_SC_TMT11plex_Phos_highpHRP_F04.raw	Raw
	20200722_HZ_SC_TMT11plex_Phos_highpHRP_F05.raw	Raw

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Publications

The Yeast Gsk-3 Kinase Mck1 Is Necessary for Cell Wall Remodeling in Glucose-Starved and Cell Wall-Stressed Cells.

Zhang Fan F Tang Yingzhi Y Zhou Houjiang H Li Kaiqiang K West James A JA Griffin Julian L JL Lilley Kathryn S KS Zhang Nianshu N

International journal of molecular sciences 20250409 8

The cell wall integrity (CWI) pathway is responsible for transcriptional regulation of cell wall remodeling in response to cell wall stress. How cell wall remodeling mediated by the CWI pathway is effected by inputs from other signaling pathways is not well understood. Here, we demonstrate that the Mck1 kinase cooperates with Slt2, the MAP kinase of the CWI pathway, to promote cell wall thickening in glucose-starved cells. Integrative analyses of the transcriptome, proteome and metabolic profili ...[more]

PMID: 40332024

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Multi-level proteomics reveals host-perturbation strategies of SARS-CoV-2 and SARS-CoV

Project description:The sudden global emergence of SARS-CoV-2 urgently requires an in-depth understanding of 39 molecular functions of viral proteins and their interactions with the host proteome. Several omics studies have extended our knowledge of COVID-19 pathophysiology, including some focused on proteomic aspects1–3. To understand how SARS-CoV-2 and related coronaviruses manipulate the host we here characterized interactome, proteome and signaling processes in a systems-wide manner. This identified connections between the corresponding cellular events, revealed functional effects of the individual viral proteins and put these findings into the context of host signaling pathways. We investigated the closely related SARS-CoV-2 and SARS-CoV viruses as well as the influence of SARS-CoV-2 on transcriptome, proteome, ubiquitinome and phosphoproteome of a lung-derived human cell line. Projecting these data onto the global network of cellular interactions revealed 48 relationships between the perturbations taking place upon SARS-CoV-2 infection at different layers and identified unique and common molecular mechanisms of SARS coronaviruses. The results highlight the functionality of individual proteins as well as vulnerability hotspots of SARS-CoV-2, which we targeted with clinically approved drugs. We exemplify this by identification of kinase inhibitors as well as MMPase inhibitors with significant antiviral effects against SARS-CoV-2

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RNA-seq of MIN6 cells overexpressing Hnf1a through CRISPR activation

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Identification of Syntaxin 7 and 12 as the first selective substrates for SGK3

Project description:Deregulation of the PI3K/Akt pathway is a common feature in many types of cancer. Recent data has demonstrated that prolonged inhibition of breast cancer cell lines with PI3K and Akt inhibitors leads to up-regulation and increased activity of the AGC kinase Serum and glucocorticoid activated kinase 3, SGK3, which in turn substitutes for Akt and leads to activation of mTORC1. SGK3 and Akt exhibit similar substrate specificity for Ser/Thr residues in the RxRxxS/T motif. However, SGK3 can be regulated by both PI3K class I and class III and possesses a unique PX domain, enabling it to bind to PI(3)P lipids in endosomes. Still, the known SGK3 substrates are either shared or have not been tested whether Akt can phosphorylate them. In the present study, we undertook genetic and pharmacologic phosphoproteomic screens to search for selective SGK3 substrates. We identified a significant number of potential in vivo SGK3 selective substrates, including the endosomal proteins STX7, STX12, RFIP4 and WDR44. In vitro phosphorylation studies demonstrated that these substrates were directly phosphorylated at the sites identified in vivo by SGK3 but, unlike all other SGK3 substrates reported, not by Akt. We provide evidence that endogenous STX7 and STX12 are physiological SGK3 substrates whose phosphorylation is potently stimulated by IGF1. Our data pinpoint that STX7 and STX12 are the first selective SGK3 substrates in vivo and this phosphorylation enhances their interaction with the respective SNARE complexes. Finally, we suggest that STX7 and STX12 phosphorylation can be utilised as in vivo biomarkers for SGK3 activity.

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Proteomics and phosphoproteomics analysis of SUM159 cells upon ClpP activation with ONC201 and TR57 compounds

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2023-05-10 | PXD038990 | Pride

Deciphering TRIM69 interactors and its phosphor-proteomic regulation in centrosome dynamics

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