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Title: Tubulin  
Author: World Heritage Encyclopedia
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Subject: Cytoskeleton, Prokaryotic cytoskeleton, Microtubule, FtsZ, Albendazole
Collection: Cytoskeleton, Proteins
Publisher: World Heritage Encyclopedia


kif1a head-microtubule complex structure in atp-form
Symbol Tubulin
Pfam PF00091
Pfam clan CL0442
InterPro IPR003008
SCOP 1tub

Tubulin (tubul- + -in) in molecular biology can refer either to the tubulin protein superfamily of globular proteins, or one of the member proteins of that superfamily. The tubulin superfamily contains six families of tubulins (alpha-, beta-, gamma-, delta-, epsilon and zeta-tubulins).[1] Tubulin is also used to specifically refer to α-tubulin and β-tubulin, the proteins that make up microtubules in eukaryotic cells. Each has a molecular weight of approximately 50,000 Daltons.[2]

Tubulin was long thought to be specific to eukaryotes. Recently, however, the prokaryotic cell division protein FtsZ was shown to be related to tubulin.[3]


  • Tubulin domains 1
  • Function 2
    • Microtubules 2.1
  • Types 3
    • α-Tubulin 3.1
    • β-Tubulin 3.2
    • γ-Tubulin 3.3
    • δ and ε-Tubulin 3.4
    • ζ-Tubulin 3.5
  • Pharmacology 4
  • Post-translational modifications 5
  • See also 6
  • References 7
  • External links 8

Tubulin domains

The Tubulin/FtsZ family, GTPase domain is an evolutionary conserved protein domain.

This GTPase protein domain is found in all tubulin chains,[4] as well as the bacterial FtsZ family of proteins.[3][5] These proteins are involved in polymer formation. Tubulin is the major component of microtubules, while FtsZ is the polymer-forming protein of bacterial cell division that forms part of a ring in the middle of the dividing cell that is required for constriction of the cell membrane and cell envelope to yield two daughter cells. FtsZ can polymerise into tubes, sheets, and rings in vitro, and is ubiquitous in bacteria and archaea.



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.[6]

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.[7] The β-tubulin subunit is exposed on the plus end of the microtubule while the α-tubulin subunit is exposed on the minus end. After the dimer is incorporated into the microtubule, the molecule of GTP bound to the β-tubulin subunit eventually hydrolyzes into GDP through inter-dimer contacts along the microtubule protofilament.[8] 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.



Human α-tubulin subtypes include:


β-tubulin in Tetrahymena sp.

All drugs that are known to bind to human tubulin bind to β-tubulin.[9] These include paclitaxel, colchicine, and the vinca alkaloids, each of which have a distinct binding site on β-tubulin.[9]

Class III β-tubulin is a microtubule element expressed exclusively in neurons,[10] and is a popular identifier specific for neurons in nervous tissue. It binds colchicine much more slowly than other isotypes of β-tubulin.[11]

β1-tubulin, sometimes called class VI β-tubulin,[12] is the most divergent at the amino acid sequence level.[13] It is expressed exclusively in megakaryocytes and platelets in humans and appears to play an important role in the formation of platelets.[13]

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.[14]

Human β-tubulins subtypes include:


γ-Tubulin, another member of the tubulin family, is important in the 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:

Members of the γ-tubulin ring complex:

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:


Zeta-tubulin is present only in kinetoplastid protozoa.[1]


Tubulins are targets for anticancer drugs like Taxol, Tesetaxel 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 microtubule formation and has applications in cancer treatment.

Post-translational modifications

When incorporated into microtubules, tubulin accumulates a number of post-translational modifications, many of which are unique to these proteins. These modifications include detyrosination, acetylation, polyglutamylation, polyglycylation, phosphorylation, ubiquitination, sumoylation, and palmitoylation.

See also


  1. ^ a b NCBI CCD cd2186
  2. ^ "tubulin in Protein sequences". EMBL-EBI. 
  3. ^ a b Nogales E, Downing KH, Amos LA, Löwe J (1998). "Tubulin and FtsZ form a distinct family of GTPases". Nat. Struct. Biol. 5 (6): 451–8.  
  4. ^ Nogales E, Wolf SG, Downing KH (1998). "Structure of the alpha beta tubulin dimer by electron crystallography". Nature 391 (6663): 199–203.  
  5. ^ Löwe J, Amos LA (1998). "Crystal structure of the bacterial cell-division protein FtsZ". Nature 391 (6663): 203–6.  
  6. ^ Williams RC, Shah C, Sackett D (1999). "Separation of tubulin isoforms by isoelectric focusing in immobilized pH gradient gels". Anal. Biochem. 275 (2): 265–7.  
  7. ^ Heald R, Nogales E (2002). "Microtubule dynamics". J. Cell. Sci. 115 (Pt 1): 3–4.  
  8. ^ Howard J, Hyman AA (2003). "Dynamics and mechanics of the microtubule plus end". Nature 422 (6933): 753–8.  
  9. ^ a b Zhou J, Giannakakou P (2005). "Targeting microtubules for cancer chemotherapy". Curr Med Chem Anticancer Agents 5 (1): 65–71.  
  10. ^ Karki R, Mariani M, Andreoli M, He S, Scambia G, Shahabi S, Ferlini C (2013). "βIII-Tubulin: biomarker of taxane resistance or drug target?". Expert Opin. Ther. Targets 17 (4): 461.  
  11. ^ Ludueña RF (1993). "Are tubulin isotypes functionally significant". Mol. Biol. Cell 4 (5): 445–457.  
  12. ^ "TUBB1 tubulin, beta 1 class VI [Homo sapiens (human)]". Gene - NCBI. 
  13. ^ a b Lecine P, et al. (2000). "Hematopoietic-specific beta 1 tubulin participates in a pathway of platelet biogenesis dependent on the transcription factor NF-E2". Blood 96 (4): 1366–1373.  
  14. ^ McNally FJ, Vale RD (1993). "Identification of katanin, an ATPase that severs and disassembles stable microtubules". Cell 75 (3): 419–29.  

External links

  • Tubulin at the US National Library of Medicine Medical Subject Headings (MeSH)
  • EC
  • protocol for purification of tubulin from bovine brain
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