Quantitative Phosphoproteomics Analysis Uncovers PAK2- and CDK1-Mediated Malignant Signaling Pathways in Clear Cell Renal Cell Carcinoma

Şentürk, Aydanur; Sahin, Ayse T.; Armutlu, Ayse; Kiremit, Murat Can; Acar, Ömer; Erdem, Selçuk; Bağbudar, Sidar; Esen, Tarık; Özlü, Nurhan

doi:10.1016/j.mcpro.2022.100417

Molecular & Cellular Proteomics

2022

DOI: 10.1016/j.mcpro.2022.100417

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Quantitative Phosphoproteomics Analysis Uncovers PAK2- and CDK1-Mediated Malignant Signaling Pathways in Clear Cell Renal Cell Carcinoma

Aydanur Şentürk

Ayse T. Sahin

Ayse Armutlu

et al.

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Cited by 3 publications

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Advancements in Global Phosphoproteomics Profiling: Overcoming Challenges in Sensitivity and Quantification

Muneer,

Chen,

Chen

2024

Proteomics

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Protein phosphorylation introduces post‐genomic diversity to proteins, which plays a crucial role in various cellular activities. Elucidation of system‐wide signaling cascades requires high‐performance tools for precise identification and quantification of dynamics of site‐specific phosphorylation events. Recent advances in phosphoproteomic technologies have enabled the comprehensive mapping of the dynamic phosphoproteomic landscape, which has opened new avenues for exploring cell type‐specific functional networks underlying cellular functions and clinical phenotypes. Here, we provide an overview of the basics and challenges of phosphoproteomics, as well as the technological evolution and current state‐of‐the‐art global and quantitative phosphoproteomics methodologies. With a specific focus on highly sensitive platforms, we summarize recent trends and innovations in miniaturized sample preparation strategies for micro‐to‐nanoscale and single‐cell profiling, data‐independent acquisition mass spectrometry (DIA‐MS) for enhanced coverage, and quantitative phosphoproteomic pipelines for deep mapping of cell and disease biology. Each aspect of phosphoproteomic analysis presents unique challenges and opportunities for improvement and innovation. We specifically highlight evolving phosphoproteomic technologies that enable deep profiling from low‐input samples. Finally, we discuss the persistent challenges in phosphoproteomic technologies, including the feasibility of nanoscale and single‐cell phosphoproteomics, as well as future outlooks for biomedical applications.

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Advancements in Global Phosphoproteomics Profiling: Overcoming Challenges in Sensitivity and Quantification

Muneer,

Chen,

Chen

2024

Proteomics

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Recent progress in quantitative phosphoproteomics

Zittlau,

Nashier,

Cavarischia-Rega

et al. 2023

Expert Review of Proteomics

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Regulation of Cancer Metastasis by PAK2

Wu,

Sarkar,

Guo

2024

IJMS

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PAK2 is a serine-threonine kinase and a member of the p21-activated kinase (PAK) family. PAK2 is activated by GTP-bound rho family GTPases, Rac, and Cdc42, and it regulates actin dynamics, cell adhesion to the extracellular matrix, and cell motility. In various types of cancers, PAK2 has been implicated in the regulation of cancer cell proliferation, cell cycle, and apoptosis. In addition, recent studies have shown that PAK2 plays an important role in cancer cell metastasis, indicating PAK2 as a potential therapeutic target. This review discusses recent discoveries on the functions of PAK2 in the regulation of various types of cancers. A better understanding of the mechanisms of function of PAK2 will facilitate future development of cancer therapies.

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Quantitative Phosphoproteomics Analysis Uncovers PAK2- and CDK1-Mediated Malignant Signaling Pathways in Clear Cell Renal Cell Carcinoma

Cited by 3 publications

References 42 publications

Advancements in Global Phosphoproteomics Profiling: Overcoming Challenges in Sensitivity and Quantification

Advancements in Global Phosphoproteomics Profiling: Overcoming Challenges in Sensitivity and Quantification

Recent progress in quantitative phosphoproteomics

Regulation of Cancer Metastasis by PAK2

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