PR01161

TUBULIN

PRINTS entry
Member databasePRINTS
PRINTS typefamily
Short nameTUBULIN

Description
Imported from IPR000217

Microtubules are polymers of tubulin, a dimer of two 55kDa subunits, designated alpha and beta
[1, 2]
. Within the microtubule lattice, α-β heterodimers associate in a head-to-tail fashion, giving rise to microtubule polarity. Fluorescent labelling studies have suggested that tubulin is oriented in microtubules with beta-tubulin toward the plus end
[3]
.

For maximal rate and extent of polymerisation into microtubules, tubulin requires GTP. Two molecules of GTP are bound at different sites, termed N and E. At the E (Exchangeable) site, GTP is hydrolysed during incorporation into the microtubule. Close to the E site is an invariant region rich in glycine residues, which is found in both chains and is thought to control access of the nucleotide to its binding site
[4]
.

Most species, excepting simple eukaryotes, express a variety of closely-related alpha- and beta-isotypes. A third family member, gamma tubulin, has also been identified in a number of species. Gamma tubulin is found at microtubule-organising centres, such as the spindle poles or the centrosome, suggesting that it is involved in minus-end nucleation of microtubule assembly
[5]
. Further eukaryotic tubulins (gamma, epsilon, zeta) that are restricted to certain lineages or species have been reported
[8, 9]
.

Bacterial and archaeal homologues of tubulin have been discovered. BtubA and BtubB, two bacterial homologues in the genus Prosthecobacter, have probably been derived by horizontal gene transfer
[6, 7]
.

References
Imported from IPR000217

1.Molecular biology and genetics of tubulin. Cleveland DW, Sullivan KF. Annu. Rev. Biochem. 54, 331-65, (1985). View articlePMID: 3896122

2.Diversity among tubulin subunits: toward what functional end? Joshi HC, Cleveland DW. Cell Motil. Cytoskeleton 16, 159-63, (1990). View articlePMID: 2194680

3.Localization of an exchangeable GTP binding site at the plus end of microtubules. Mitchison TJ. Science 261, 1044-7, (1993). View articlePMID: 8102497

4.Tubulin sequence region beta 155-174 is involved in binding exchangeable guanosine triphosphate. Hesse J, Thierauf M, Ponstingl H. J. Biol. Chem. 262, 15472-5, (1987). View articlePMID: 3680207

5.Gamma-tubulin: the hub of cellular microtubule assemblies. Joshi HC. Bioessays 15, 637-43, (1993). View articlePMID: 8274140

6.Genes for the cytoskeletal protein tubulin in the bacterial genus Prosthecobacter. Jenkins C, Samudrala R, Anderson I, Hedlund BP, Petroni G, Michailova N, Pinel N, Overbeek R, Rosati G, Staley JT. Proc. Natl. Acad. Sci. U.S.A. 99, 17049-54, (2002). View articlePMID: 12486237

7.Structure of bacterial tubulin BtubA/B: evidence for horizontal gene transfer. Schlieper D, Oliva MA, Andreu JM, Lowe J. Proc. Natl. Acad. Sci. U.S.A. 102, 9170-5, (2005). View articlePMID: 15967998

8.Six subgroups and extensive recent duplications characterize the evolution of the eukaryotic tubulin protein family. Findeisen P, Muhlhausen S, Dempewolf S, Hertzog J, Zietlow A, Carlomagno T, Kollmar M. Genome Biol Evol 6, 2274-88, (2014). View articlePMID: 25169981

9.Zeta-Tubulin Is a Member of a Conserved Tubulin Module and Is a Component of the Centriolar Basal Foot in Multiciliated Cells. Turk E, Wills AA, Kwon T, Sedzinski J, Wallingford JB, Stearns T. Curr Biol 25, 2177-83, (2015). PMID: 26234217

Supplementary References

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