Dataset Information

System-wide identification and prioritization of enzyme substrates by thermal analysis (SIESTA)

ABSTRACT: Despite the immense importance of enzyme-substrate reactions, there is a lack of generic and unbiased tools for identifying and prioritizing substrate proteins which are modulated in the structural and functional levels through modification. Here we describe a high-throughput unbiased proteomic method called System-wide Identification and prioritization of Enzyme Substrates by Thermal Analysis (SIESTA). The approach assumes that enzymatic post-translational modification of substrate proteins might change their thermal stability. SIESTA successfully identifies several known and novel substrate candidates for selenoprotein thioredoxin reductase 1, protein kinase B (AKT1) and poly-(ADP-ribose) polymerase-10 systems in up to a depth of 7,179 proteins. Wider application of SIESTA can enhance our understanding of the role of enzymes in homeostasis and disease, open new opportunities in investigating the effect of PTMs on signal transduction and facilitate drug discovery.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Uterine Cervix, Epithelial Cell Of Cervix

DISEASE(S): Cervix Carcinoma

SUBMITTER: Amir Ata Saei

LAB HEAD: Prof. Roman A. Zubarev

PROVIDER: PXD021916 | Pride | 2021-01-11

REPOSITORIES: Pride

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System-wide identification and prioritization of enzyme substrates by thermal analysis.

Saei Amir Ata AA Beusch Christian M CM Sabatier Pierre P Wells Juan Astorga JA Gharibi Hassan H Meng Zhaowei Z Chernobrovkin Alexey A Rodin Sergey S Näreoja Katja K Thorsell Ann-Gerd AG Karlberg Tobias T Cheng Qing Q Lundström Susanna L SL Gaetani Massimiliano M Végvári Ákos Á Arnér Elias S J ESJ Schüler Herwig H Zubarev Roman A RA

Nature communications 20210226 1

Despite the immense importance of enzyme-substrate reactions, there is a lack of general and unbiased tools for identifying and prioritizing substrate proteins that are modified by the enzyme on the structural level. Here we describe a high-throughput unbiased proteomics method called System-wide Identification and prioritization of Enzyme Substrates by Thermal Analysis (SIESTA). The approach assumes that the enzymatic post-translational modification of substrate proteins is likely to change the ...[more]

PMID: 33637753

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	AKT1_inhibitors_03.raw	Raw