An α-tubulin mutant destabilizes the heterodimer: Phenotypic consequences and interactions with tubulin-binding proteins

Molecular Biology of the Cell

Volumn 9, Issue 9, 1998, Pages 2349-2360

  Vega, Leticia R ^a   Fleming, James ^a   Solomon, Frank ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA TUBULIN; BINDING PROTEIN; DIMER; MUTANT PROTEIN;

ARTICLE; COLD SENSITIVITY; CONTROLLED STUDY; HAPLOIDY; HETEROZYGOTE; LETHALITY; MICROTUBULE ASSEMBLY; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN POLYMERIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; SACCHAROMYCES CEREVISIAE;

SACCHAROMYCES CEREVISIAE;

EID: 0031671082     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.9.9.2349     Document Type: Article

References (38)

1. Alvarez, P., Smith, A., Fleming, J., and Solomon, F. (1998). Modulation of tubulin polypeptide ratios by the yeast protein Pac10p. Genetics 149, 857-864.
2. Archer, J., Magendantz, M., Vega, L., and Solomon, F. (1998). Formation and function of the Rbl2p-β-tubulin complex. Mol. Cell. Biol. 18, 1757-1762.
3. Archer, J.E., Vega, L.R., and Solomon, F. (1995). Rbl2p, a yeast protein that binds to β-tubulin and participates in microtubule function in vivo. Cell 82, 425-434.
4. Bond, J.F., Fridovich-Keil, J.L., Pillus, L., Mulligan, R.C., and Solomon, F. (1986). A chicken-yeast chimeric β-tubulin protein is incorporated into mouse microtubules in vivo. Cell 44, 461-468.
5. Caceres, A., and Kosik, K. (1990). Inhibition of neurite polarity by tau antisense oligonucleotides in primary cerebellar neurons. Nature 343, 461-463.
6. Chen, X., Sullivan, D., and Huffaker, T. (1994). Two yeast genes with similarity to TCP-1 are required for microtubule and actin function in vivo. Proc. Natl. Acad. Sci. USA 91, 9111-9115.
7. Dinsmore, J., and Solomon, F. (1991). Inhibition of Map2 expression affects both morphological and cell division phenotypes of neuronal differentiation. Cell 64, 817-826.
8. Fuller, M.T., Caulton, J.H., Hutchens, J.A., Kaufman, T.C., and Raff, E.C. (1987). Genetic analysis of microtubule structure: A β-tubulin mutation causes the formation of aberrant microtubules in vivo and in vitro. J. Cell Biol. 104, 385-394.
9. Geiser, J.R., Schott, E.J., Kingsbury, T.J., Cole, N.B., Totis, L.J., Bhattacharyya, G., He, L., and Hoyt, M.A. (1997). Saccharomyces cerevisiae genes required in the absence of the CIN8-encoded spindle motor act in functionally diverse mitotic pathways. Mol. Biol. Cell 8, 1035-1050.
10. Geissler, S., Siegers, K., and Schiebel, E. (1998). A novel protein complex promoting formation of functional α-and γ-tubulin. EMBO J. 17, 952-966.
11. Guénette, S., Magendantz, M., and Solomon, F. (1995). BUB1 and BUB3 are multicopy suppressors of a Saccharomyces cerevisiae α-tubulin mutation that causes a microtubule assembly defect. J. Cell Sci. 108, 1195-1204.
12. Hirata, D., Masuda, H., Eddison, M., and Toda, T. (1998). Essential role of tubulin-rolding cofactor D in microtubule assembly and its association with microtubules in fission yeast. EMBO J. 17, 656-666.
13. Hoyle, H.D., and Raff, E.C. (1990). Two Drosophila beta tubulin isoforms are not functionally equivalent. J. Cell Biol. 111, 1009-1026.
14. Hoyt, M., Macke, J., Roberts, B., and Geiser, J. (1997). Saccharomyces cerevisiae PAC2 functions with CIN1, 2 and 4 in a pathway leading to normal microtubule stability. Genetics 146, 849-857.
15. Hoyt, M., Stearns, T., and Botstein, D. (1990). Chromosome instability mutants of Saccharomyces cerevisiae that are defective in microtubule-mediated processes. Mol. Cell. Biol. 10, 223-234.
16. Huffaker, T., Thomas, J., and Botstein, D. (1988). Diverse effects of beta-tubulin mutations on microtubule formation and function. J. Cell Biol. 106, 1997-2010.
17. Joshi, H.C., and Cleveland, D.W. (1989). Differential utilization of β-tubulin isotypes in differentiating neuntes. J. Cell Biol. 109, 663-673.
18. Katz, W., Weinstein, B., and Solomon, F. (1990). Regulation of tubulin levels and microtubule assembly in Saccharomyces cerevisiae: consequences of altered tubulin gene copy number in yeast. Mol. Cell. Biol. 10, 2730-2736.
19. Kirkpatrick, D., and Solomon, F. (1994). Overexpression of yeast homologs of the mammalian checkpoint gene RCC1 suppresses the class of α-tubulin mutations that arrest with excess microtubules. Genetics 137, 381-392.
20. Magendantz, M., Henry, M., Lander, A., and Solomon, F. (1995). Inter-domain interactions of radixin in vitro. J. Biol. Chem. 270, 25324-25327.
21. Melki, R., Rommelaere, H., Leguy, R., Vandekerckhove, J., and Ampe, C. (1996). Cofactor A is a molecular chaperone required for beta-tubulin folding: functional and structural characterization. Biochemistry 35, 10422-10435.
22. Mitchison, T., and Kirschner, M. (1984). Dynamic instability of microtubule growth. Nature 312, 237-242.
23. Nogales, E., Wolf, S., and Downing, K. (1998). Structure of the αβ tubulin dimer by electron crystallography. Nature 391, 199-203.
24. Oakley, B., and Morris, N.R. (1980). Nuclear movement is beta tubulin-dependent in Aspergillus nidulans. Cell 19, 255-262.
25. Pachter, J.S., Yen, T.J., and Cleveland, D.W. (1987). Autoregulation of tubulin expression is achieved through specific degradation of polysomal tubulin mRNAs. Cell 51, 283-292.
26. Praitis, V., Katz, W.S., and Solomon, F. (1991). A codon change in β-tubulin which drastically affects microtubule structure in Drosophila melanogaster fails to produce a significant phenotype in Saccharomyces cerevisiae. Mol. Cell. Biol. 11, 4726-4731.
27. Saxton, W.M., Stemple, D.L., Leslie, R.J., Salmon, E.D., Zavortink, M., and McIntosh, J.R. (1984). Tubulin dynamics in cultured mammalian cells. J. Cell Biol. 99, 2175-2186.
28. Schatz, P.J., Solomon, F., and Botstein, D. (1986). Genetically essential and nonessential α-tubulin genes specify functionally interchangeable proteins. Mol. Cell. Biol. 6, 3722-3733.
29. Sherman, F., Fink, G., and Hicks, J. (1986). Laboratory Course Manual for Methods in Yeast Genetics, Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.
30. Sikorski, R.S., and Hieter, P. (1989). A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27.
31. Solomon, F., Connell, L., Kirkpatrick, D., Praitis, V., and Weinstein, B. (1992). Methods for studying the yeast cytoskeleton. In: The Cytoskeleton, ed. K. Carraway and C. Carraway, Oxford, United Kingdom: Oxford University Press, 197-222.
32. Stearns, T., Hoyt, M., and Botstein, D. (1990). Yeast mutants sensitive to anti-microtubule drugs define three genes that affect microtubule function. Genetics 124, 251-262.
33. Sullivan, D., and Huffaker, T. (1992). Astral microtubules are not required for anaphase B in Saccharomyces cerevisiae. J. Cell Biol. 119, 379-388.
34. Tian, G., Huang, Y., Rommelaere, H., Vandekerckhove, J., Ampe, C., and Cowan, N. (1996). Pathway leading to correctly folded β-tubulin. Cell 86, 287-296.
35. Tian, G., Lewis, S., Feierbach, B., Stearns, T., Rommelaere, H., Ampe, C., and Cowan, N. (1997). Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors. J. Cell Biol. 138, 821-832.
36. Ursic, D., and Culbertson, M. (1991). The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes. Mol. Cell. Biol. 11, 2629-2640.
37. Velculescu, V., Zhang, L., Zhou, W., Vogelstein, J., Basrai, M., Bassett, D., Hieter, P., Vogelstein, B., and Kinzler, K. (1997). Characterization of the yeast transcriptome. Cell 88, 243-251.
38. Weinstein, B., and Solomon, F. (1990). Phenotypic consequences of tubulin overproduction in Saccharomyces cerevisiae: differences between alpha-tubulin and beta-tubulin. Mol. Cell. Biol. 10, 5295-5304.