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Microtubule dynamics.

¹Department of Biochemistry, University of North Carolina, Chapel Hill 27599-7260.

Current Opinion in Cell Biology

|February 1, 1992

Summary

This summary is machine-generated.

Microtubule structure heterogeneity is not definitively proven to stem from tubulin-GDP and tubulin-GTP. Dynamic behavior suggests tubulin-GDP exists in two conformations within microtubules.

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Area of Science:

Biochemistry
Cell Biology
Structural Biology

Background:

Compelling evidence suggests heterogeneity in microtubule subunit structure.
The precise cause, specifically the presence of tubulin-GDP and tubulin-GTP within polymers, remains unproven.

Purpose of the Study:

To investigate the structural heterogeneity of microtubule subunits.
To explore the role of tubulin-GDP and tubulin-GTP in microtubule dynamics.
To discuss microtubule-associated protein interactions and phosphorylation.

Main Methods:

Analysis of microtubule subunit conformations.
Mechanistic modeling of microtubule dynamics.
Discussion of protein binding and phosphorylation effects.

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Main Results:

Evidence suggests excluding a monolayer of tubulin-GTP at microtubule ends.
Microtubule dynamics are best explained by tubulin-GDP existing in two conformations.
Mechanisms of microtubule-associated protein binding and phosphorylation are discussed.

Conclusions:

The heterogeneity in microtubule structure may not solely result from tubulin-GDP and tubulin-GTP presence.
A model involving two tubulin-GDP conformations explains microtubule dynamics.
Microtubule-associated protein interactions and phosphorylation play roles in microtubule function.