Related Experiment Video
Updated: May 21, 2026
12:47
Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
Published on: December 27, 2016
Tau Phosphorylation by GSK3 in Different Conditions
Jesús Avila1, Gonzalo León-Espinosa, Esther García
1Centro de Biologia Molecular "Severo Ochoa" (CSIC-UAM), Nicolás Cabrera 1, Campus Cantoblanco UAM, 28049 Madrid, Spain.
International Journal of Alzheimer'S Disease
|June 8, 2012
Summary
Tau protein phosphorylation, particularly on serine/threonine residues, has dual roles. It can be protective in states like hibernation but toxic in tauopathies, leading to hyperphosphorylation and aggregation.
Area of Science:
- Biochemistry
- Neuroscience
- Cell Biology
Background:
- Tau protein is crucial for microtubule stability.
- A significant portion of tau residues are phosphorylatable (serine, threonine, tyrosine).
- Phosphorylation status significantly impacts tau protein function and pathology.
Purpose of the Study:
- To explore the consequences of tau protein being a phosphoprotein.
- To focus on the role of serine/threonine phosphorylation in tau.
- To discuss the dualistic nature of tau phosphorylation in biological processes and disease.
Main Methods:
- Review and commentary on existing literature regarding tau phosphorylation.
- Analysis of the impact of specific residue modifications.
- Correlation of phosphorylation patterns with physiological and pathological states.
Main Results:
- Phosphorylation of tau protein can be either protective or detrimental.
- Specific serine/threonine phosphorylation sites influence tau's role.
- Hyperphosphorylation and aggregation of tau are hallmarks of tauopathies.
Conclusions:
- Tau phosphorylation is a critical regulatory mechanism with context-dependent outcomes.
- Understanding tau phosphorylation is key to deciphering tauopathies.
- Targeting tau phosphorylation may offer therapeutic strategies for neurodegenerative diseases.
Related Concept Videos
01:02Phosphorylation
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...
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...
01:22PI3K/mTOR/AKT Signaling Pathway
The mammalian target of rapamycin (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1 (mTORC1) and mTOR complex 2 (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast, mTORC2 consists of a rapamycin-insensitive companion...
02:54Protein Kinases and Phosphatases
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...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
02:54Protein Kinases and Phosphatases
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...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
01:22Amplifying Signals via Enzymatic Cascade
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 the...
01:25cAMP-dependent Protein Kinase Pathways
Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...