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Multisite phosphorylation of tau proteins from rat brain
Biochemical and Biophysical Research Communications
|August 30, 1983
Summary
Tau proteins in rat brains undergo multisite phosphorylation by various protein kinases. Different kinases target distinct sites on tau, highlighting its complex regulatory modifications.
Area of Science:
- Neuroscience
- Molecular Biology
- Biochemistry
Background:
- Tau proteins are crucial for microtubule stability in neurons.
- Aberrant tau phosphorylation is implicated in neurodegenerative diseases like Alzheimer's.
Purpose of the Study:
- To investigate the in vitro phosphorylation of tau proteins.
- To identify the kinases involved and the sites of phosphorylation on tau.
Main Methods:
- In vitro phosphorylation assays using tau proteins from adult and young rat brains.
- Incubation with endogenous protein kinases from microtubule preparations.
- Treatment with specific kinases: cyclic AMP-dependent protein kinase and casein kinase type I.
Main Results:
- Multiple phosphate groups were incorporated into different molecular species of tau proteins.
- Cyclic AMP-dependent protein kinase and casein kinase type I phosphorylated tau at distinct sites.
- Tau proteins serve as substrates for multiple phosphorylation events.
Conclusions:
- Tau proteins are subject to multisite phosphorylation.
- The specific sites of phosphorylation can be influenced by the type of protein kinase involved.
- Understanding tau phosphorylation is critical for comprehending its role in neuronal function and disease.