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Tau complexes with phospholipase C-gamma in situ
1Department of Psychiatry and Behavioral Neurobiology, University of Alabama at Birmingham, 35294-0017, USA.
Neuroreport
|May 20, 1998
Summary
Tau protein may regulate cell signaling by interacting with phospholipase C-gamma (PLC-gamma). This study confirms a tau-PLC-gamma complex in human cells, suggesting tau’s role in PLC-gamma pathway signaling in vivo.
Area of Science:
- Neuroscience
- Cell Biology
- Molecular Biology
Background:
- Recent in vitro studies suggest tau protein's involvement in signal transduction via the phospholipase C-gamma (PLC-gamma) pathway.
- The precise in vivo function of tau in this signaling cascade remains to be fully elucidated.
Purpose of the Study:
- To investigate the physiological relevance of tau's interaction with the PLC-gamma signaling pathway.
- To demonstrate the existence and characterize the nature of a tau-PLC-gamma complex in situ within a human neuroblastoma cell line.
Main Methods:
- Co-purification of proteins associated with microtubule-associated proteins.
- Co-immunoprecipitation assays to detect protein-protein interactions.
- Enzymatic activity assays on immunoprecipitated PLC.
Main Results:
- PLC-gamma and PLC-delta, but not PLC-beta, co-purified with microtubule-associated proteins.
- PLC-gamma, but not PLC-delta or PLC-beta, co-immunoprecipitated with tau.
- Enzymatically active PLC was found to co-precipitate with tau.
- Both tau and MAP-2 (microtubule-associated protein 2) co-precipitated with PLC-gamma.
Conclusions:
- Tau directly or indirectly associates with PLC-gamma in situ.
- This interaction suggests tau's localization is appropriate for regulating signal transduction through the PLC-gamma pathway in vivo.
- The findings support the hypothesis of tau's role in PLC-gamma mediated cellular signaling.