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7.4: Microtubules

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    Microtubules are made up of two equally distributed, structurally similar, globular subunits: α and β tubulin. Like microfilaments, microtubules are also dependent on a nucleotide triphosphate for polymerization, but in this case, it is GTP.

    Microtubule stability is temperature-dependent: if cooled to 4°C, microtubules fall apart into αβ-tubulin heterodimers. Warmed back up to 37°C, the tubulin repolymerizes if there is GTP available.

    Another similarity is that microtubules have a polarity in which the (-) end is far less active than the (+) end. However, unlike the twisted-pair microfilaments, the microtubules are mostly found as large 13-stranded (each strand is called a protofilament) hollow tube structures. Also, the α and β tubulin used for building the microtubules not only alternate, but they are actually added in pairs. Both the α-tubulin and β-tubulin must bind to GTP to associate, but once bound, the GTP bound to α-tubulin does not move. On the other hand, GTP bound in the β-tubulin may be hydrolyzed to GDP. GDP-bound αβ-dimers will not be added to a microtubule, so similar to the situation with ATP and g-actin, if the tubulin has GDP bound to it, it must first exchange it for a GTP before it can be polymerized. Although the affinity of tubulin for GTP is higher than the affinity for GDP, this process is usually facilitated by a GEF, or guanine nucleotide exchange factor. As the signal transduction chapter will show in more detail, this type of nucleotide exchange is a common mechanism for activation of various biochemical pathways.

    Screen Shot 2019-01-07 at 6.54.09 PM.png
    Figure \(\PageIndex{4}\). Microtubules exhibit dynamic instability. GTP-bound αβ-tubulin dimers are added onto the microtubule. Once the GTP is hydrolyzed, the conformational shift strains the microtubule, which will tend to break apart unless new tubulin dimers are added to stabilize the structure.

    Again like actin, the tubulin itself has enzymatic activity, and over time, the GTPase activity hydrolyzes the GTP to GDP and phosphate. This changes the attachment between β-tubulin of one dimer and the α-tubulin of the dimer it is stacked on because the shape of the subunit changes. Even though it isn’t directly loosening its hold on the neighboring tubulin, the shape change causes increased stress as that part of the microtubule tries to push outward. This is the basis of a property of microtubules known as dynamic instability. If there is nothing to stabilize the microtubule, large portions of it will fall apart. However, as long as new tubulin (which will have GTP bound) is being added at a high enough rate to keep a section of low-stress “stable”-conformation microtubule (called the GTP cap) on top of the older GDP-containing part, then it stabilizes the overall microtubule. When new tubulin addition slows down, and there is only a very small or nonexistent cap, then the microtubule undergoes a catastrophe in which large portions rapidly break apart. Note that this is a very different process than breakdown by depolymerization, which is the gradual loss of only a few subunits at a time from an end of the microtubule. Depolymerization also occurs, and like with actin, is determined partially by the relative concentrations of free tubulin and microtubules.

    From a physical standpoint, the microtubule is fairly strong, but not very flexible. A microfilament will flex and bend when a deforming force is applied (imagine the filament anchored at the bottom end standing straight up, and something pushing the tip to one side). The microtubule in the same situation will bend only slightly, but break apart if the deforming force is sufficient. There is, of course, a limit to the flexibility of the microfilament and eventually, it will also break. Intermediate filaments are slightly less flexible than the microfilaments, but can resist far more force that either microfilaments or microtubules.

    This page titled 7.4: Microtubules is shared under a CC BY-NC-SA 3.0 license and was authored, remixed, and/or curated by E. V. Wong via source content that was edited to the style and standards of the LibreTexts platform; a detailed edit history is available upon request.