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Tubulin: Wikis


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Molecular structure of a tubulin dimer. The α-tubulin subunit is on top, indicating a microtubule polarity with the (-) end towards the top of the page. The two GTP subunits are drawn as space filling models, and the paclitaxel molecule is attached to the β-tubulin subunit and drawn as a ball and stick model.

Tubulin is one of several members of a small family of globular proteins. The most common members of the tubulin family are α-tubulin and β-tubulin, the proteins that make up microtubules. Each has a molecular weight of approximately 55 kiloDaltons. Microtubules are assembled from dimers of α- and β-tubulin. These subunits are slightly acidic with an isoelectric point between 5.2 and 5.8.[1]

Tubulin was long thought to be specific to eukaryotes. Recently, however, the prokaryotic cell division protein FtsZ was shown to be evolutionarily related to tubulin.[2]


α-tubulin and β-tubulin

To form microtubules, the dimers of α- and β-tubulin bind to GTP and assemble onto the (+) ends of microtubules while in the GTP-bound state.[3] After the dimer is incorporated into the microtubule, the molecule of GTP bound to the β-tubulin subunit eventually hydrolyses into GDP through inter-dimer contacts along the microtubule protofilament.[4]. Whether the β-tubulin member of the tubulin dimer is bound to GTP or GDP influences the stability of the dimer in the microtubule.

Dimers bound to GTP tend to assemble into microtubules, while dimers bound to GDP tend to fall apart; thus, this GTP cycle is essential for the dynamic instability of the microtubule.

Class III β-tubulin‎ is a microtubule element expressed exclusively in neurons, and is a popular identifier specific for neurons in nervous tissue.

Katanin is a protein complex that severs microtubules at β-tubulin subunits, and is necessary for rapid microtubule transport in neurons and in higher plants.[5]

Human α- and β-tubulin subtypes include:[6]

β-tubulin in Tetrahymena sp.


γ-tubulin, another member of the tubulin family, is important in the nucleation and polar orientation of microtubules. It is found primarily in centrosomes and spindle pole bodies, since these are the areas of most abundant microtubule nucleation. In these organelles, several γ-tubulin and other protein molecules are found in complexes known as γ-tubulin ring complexes (γ-TuRCs), which chemically mimic the (+) end of a microtubule and thus allow microtubules to bind. γ-tubulin also has been isolated as a dimer and as a part of a γ-tubulin small complex (γTuSC), intermediate in size between the dimer and the γTuRC. γ-tubulin is the best understood mechanism of microtubule nucleation, but certain studies have indicated that certain cells may be able to adapt to its absence, as indicated by mutation and RNAi studies that have inhibited its correct expression.

Human γ-tubulin subtypes include:[6]

δ and ε tubulin

Delta (δ) and epsilon (ε) tubulin have been found to localize at centrioles and may play a role in forming the mitotic spindle during mitosis, though neither is as well-studied as the α- and β- forms.

Human δ- and ε-tubulin subtypes include:[6]

  • δ-tubulin
    • TUBD1
  • ε-tubulin
    • TUBE1


Tubulins are targets for anticancer drugs like Taxol and the "Vinca alkaloid" drugs such as vinblastine and vincristine. The anti-gout agent colchicine binds to tubulin and inhibits microtubule formation, arresting neutrophil motility and decreasing inflammation. The anti-fungal drug Griseofulvin targets mictotubule formation and has applications in cancer treatment.

See also


  1. ^ Williams RC Jr, Shah C, Sackett D (November 1999). "Separation of tubulin isoforms by isoelectric focusing in immobilized pH gradient gels". Anal Biochem 275 (2): 265–7. doi:10.1006/abio.1999.4326. PMID 10552916.  
  2. ^ Nogales E, Downing KH, Amos LA, Löwe J (June 1998). "Tubulin and FtsZ form a distinct family of GTPases". Nat Struct Biol 5 (6): 451–8. doi:10.1038/nsb0698-451. PMID 9628483.  
  3. ^ Heald R, Nogales E (January 2002). "Microtubule dynamics". J Cell Sci 115 (Pt 1): 3–4. PMID 11801717.  
  4. ^ Howard J, Hyman AA (April 2003). "Dynamics and mechanics of the microtubule plus end". Nature 422 (6933): 753–8. doi:10.1038/nature01600. PMID 12700769.  
  5. ^ McNally FJ, Vale RD (November 1993). "Identification of katanin, an ATPase that severs and disassembles stable microtubules". Cell 75 (3): 419–29. PMID 8221885.  
  6. ^ a b c Dutcher SK (February 2001). "The tubulin fraternity: alpha to eta". Curr Opin Cell Biol 13 (1): 49–54. PMID 8221885.  

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