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PMID:6425287
| Citation |
Lindwall, G and Cole, RD (1984) Phosphorylation affects the ability of tau protein to promote microtubule assembly. J. Biol. Chem. 259:5301-5 |
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| Abstract |
Tau is a family of closely related proteins known for its ability to copolymerize with tubulin, inducing the formation of microtubules. When tau was stripped of phosphate by treatment with alkaline phosphatase it underwent a pronounced change in electrophoretic mobility, probably reflecting a conformational change. The dephosphorylated tau promoted significantly more rapid and more extensive polymerization of microtubules though there was no obvious difference in the microtubules formed. Partially purified microtubule protein contains a kinase that can rephosphorylate tau. |
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| Keywords |
Alkaline Phosphatase; Animals; Brain/metabolism; Cattle; Kinetics; Macromolecular Substances; Microscopy, Electron; Microtubules/metabolism; Microtubules/ultrastructure; Nerve Tissue Proteins/metabolism; Phosphorylation; Proteins/isolation & purification; Proteins/metabolism; Tubulin/metabolism; tau Proteins |
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Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0006468: protein phosphorylation |
ECO:0000314: |
P |
Figure 1 and 2 showed the electrophoresis of the results of dephosphorylating tau in different conditions and reversing that process, respectively. The analysis revealed a change in eletrophoretic mobility, showing that tau can exist in two separate states that are readily interconvertible by phosphorylation and dephosphorylation. |
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See also
References
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