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Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
13.7K
Proteomics01:33

Proteomics

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A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
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Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

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When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
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Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

8.9K
Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
8.9K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

6.0K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
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Phosphorylation01:02

Phosphorylation

52.1K
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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Updated: Oct 11, 2025

Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer
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Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer

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Personalized phosphoproteomics identifies functional signaling.

Elise J Needham1, Janne R Hingst2, Benjamin L Parker1,3

  • 1Charles Perkins Centre, School of Life and Environmental Sciences, University of Sydney, Sydney, New South Wales, Australia.

Nature Biotechnology
|December 3, 2021
PubMed
Summary
This summary is machine-generated.

Personalized phosphoproteomics links cellular signaling to biological function using individual differences. This approach identified new protein phosphorylation sites and a novel interaction between mTOR and AMPK in muscle metabolism.

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Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer
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Area of Science:

  • Molecular Biology
  • Systems Biology
  • Metabolomics

Background:

  • Protein phosphorylation is a key regulatory mechanism integrating cellular signals.
  • Identifying functional phosphosites amidst global changes is challenging.
  • Human phenotypic variance offers a unique lens for biological investigation.

Purpose of the Study:

  • To introduce 'personalized phosphoproteomics' for linking signaling to function.
  • To investigate exercise-induced insulin signaling in human skeletal muscle.
  • To uncover novel regulatory pathways in metabolic processes.

Main Methods:

  • Combined experimental and computational analyses.
  • Measured individual phosphoproteome responses to interventions.
  • Correlated phosphoproteomic data with parallel phenotypic measurements.

Main Results:

  • Identified known and novel phosphosites in glucose metabolism proteins.
  • Discovered a cooperative relationship between mTOR and AMPK.
  • Demonstrated direct phosphorylation of AMPK by mTOR at S377, impacting metabolic regulation.

Conclusions:

  • Personalized phosphoproteomics is a robust approach for dissecting signal transduction.
  • This method can reveal functional roles of phosphosites in complex biological systems.
  • Uncovered a novel mTOR-AMPK interaction critical for metabolic adaptation.