PMID:1396588

Citation	Kanai, Y, Chen, J and Hirokawa, N (1992) Microtubule bundling by tau proteins in vivo: analysis of functional domains. EMBO J. 11:3953-61
Abstract	Tau varies both in the N-terminal region (three types) and in the C-terminal repeated microtubule binding domain (two types), generating six isoforms through alternative splicing. To understand the differences between the isoforms and to determine which domains are important for microtubule bundling, we performed transfection studies on fibroblasts using tau isoforms and deletion mutants to quantify their ability to bundle microtubules. By comparing the isoforms, we found that a longer N-terminal region induced microtubule bundling more efficiently, but changes in the microtubule binding domain did not. Mutants lacking the proline rich region or the repeated domain did not bind to microtubules. Although all the other mutants could bind to and bundle microtubules, deletion in the N-terminal neutral region or the first half of the C-terminal tail caused a significant decrease in microtubule bundling, indicating the importance of these regions in microtubule bundling.
Links	PubMed PMC556906
Keywords	Animals; Antibodies, Monoclonal; Electrophoresis, Polyacrylamide Gel; Fluorescent Antibody Technique; Immunoblotting; L Cells (Cell Line); Mice; Microtubules/ultrastructure; Mutagenesis, Site-Directed; Sequence Deletion; Terminator Regions, Genetic; Transfection; tau Proteins/analysis; tau Proteins/genetics; tau Proteins/metabolism
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
RAT:TAU	part_of	GO:0005874: microtubule	ECO:0000314: direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
RAT:TAU		GO:0005874: microtubule	ECO:0000314:		C		Figure 3 shows that Tau was localized to microtubules using an anti-Tau and an anti-tubulin antibody.	complete CACAO 9307

References

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