| Literature DB >> 35612740 |
Brianna Ball1, Jonathan R Krieger2, Jennifer Geddes-McAlister3.
Abstract
Phosphorylation is a key post-translational modification central to the biological behavior of proteins. This reversible modification specifically regulates cell signaling mechanisms to control survival and growth. Moreover, microbial pathogens, including both fungi and bacteria, rely on this modification to coordinate protein production and functioning during infection and dissemination within a host. Understanding phosphorylation and its involvement with effector proteins and complex networks are now possible with the recent technological advancements of mass spectrometry. Herein, we describe a phosphopeptide enrichment strategy optimized for the invasive mycosis-causing fungal pathogen Cryptococcus neoformans. Our protocol details proper sample preparation for efficient lysis and protein extraction with minimal phosphorylation losses followed by outlined steps for enrichment, instrumentation handling, and data analysis to permit deep profiling of the global phosphoproteome. The high-throughput versatility of bottom-up proteomics combined with our sample preparation approach facilitates opportunities for in-depth phosphorylation mapping and novel biological discoveries.Entities:
Keywords: Cell signaling; Cryptococcus neoformans; Fungal pathogens; Phosphoproteomics; Phosphorylation; Quantitative mass spectrometry
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Year: 2022 PMID: 35612740 DOI: 10.1007/978-1-0716-2124-0_10
Source DB: PubMed Journal: Methods Mol Biol ISSN: 1064-3745