Detyrosination of alpha tubulin does not stabilize microtubules in vivo [published erratum appears in J Cell Biol 1990 Sep;111(3):1325-6]

Webster, Daniel R.; Wehland, Juergen; Weber, Klaus; Borisy, Gary G.

doi:10.1083/jcb.111.1.113

Cited by 141 publications

(30 citation statements)

References 56 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Our data corroborated results of Khawaja et al (7) and Webster et al (8), who showed that detyrosination is a result of, rather than a contributor to, MT stabilization. The specificity of NO 2 Tyr allowed us to test independently the role of a single post-translational modification.…”

Section: Discussionsupporting

confidence: 83%

See 1 more Smart Citation

Alteration of the C-terminal Amino Acid of Tubulin Specifically Inhibits Myogenic Differentiation

Chang¹,

Webster²,

Salam³

et al. 2002

Journal of Biological Chemistry

View full text Add to dashboard Cite

Section: Discussionsupporting

confidence: 83%

“…MTs enriched in Glu tubulin (called Glu MTs) have been shown to be enhanced in cellular longevity or stability (4 -6). However, detyrosination is known to be insufficient to stabilize MTs (7,8), rendering detyrosination an effect, not a cause, of MT stability.…”

Section: Microtubules (Mts)mentioning

confidence: 99%

Alteration of the C-terminal Amino Acid of Tubulin Specifically Inhibits Myogenic Differentiation

Chang¹,

Webster²,

Salam³

et al. 2002

Journal of Biological Chemistry

View full text Add to dashboard Cite

“…Since there are specific antibodies against these two forms oftubulin (13), it is a simple matter to probe the location of dynamic and stable MTs in vivo: MTs that have accumulated sufficient Glu-tubulin to be detected with an antibody to Glu-tubulin (termed Glu-MTs) are operationally defined as stable MTs; those that lack Glu-tubulin immunoreactivity but stain with an antibody to Tyr-tubulin (termed Tyr-MTs) are operationally defined as dynamic MTs. While the different levels ofposttranslationally modified tubulin could account for differences in the stability of MTs, experiments to date indicate that elevated levels of Glu-tubulin in MTs do not cause MT stability (14,15). An alternative mechanism by which Glu-MTs could be stabilized is suggested by the observation that Glu-MTs are refractory to subunit addition and loss (7,14); thus, they behave as if they were capped in vivo.…”

mentioning

confidence: 99%

Protein phosphatase inhibitors induce the selective breakdown of stable microtubules in fibroblasts and epithelial cells.

Gurland

Gundersen

1993

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

In many cell types, a small subset of mlcrotubules (MfTs) are unusually long-lived compared with the majority of the MTs. These "stable" MTs may be Important mediators ofdifferentative events sice they are usualy found alined with developing asymmetries of cels undergoing morphogenesis. In additin to their longevity, the stable MTs are more resitant to drug depolymerization and are enriched in posttransatonally detyrosinated tubulin (Glu-tubulin). To determine the role of protein phosphorylatlon in the regulation of these stable MTs, we treated NIH 3T3 fibroblasts and TC-7 moukey kidney epitheal cells with okadaic acid (OA) and calyculn A, potent hibitors of protein phosphatases 1 and 2A (PP1 and PP2A), and then localized dynamic MTs and stable MTs with antibodies specfflc for tyrosinated tubuln (Tyrtubulin) and Glu-tubulHn, respectively. OA at 0.1-10 pM caused a rapid and complete breakdown of Glu-MTs (MTs enriched in Glu-tubulin) in both cell types without substantially aecting the number of Tyr-MTs. While all concentrations of OA over this range resulted in a complete loss of Glu-MTs, the onset of Glu-MT breakdown was proportional to the loprithm ofthe OA concentration. The inactive analog of OA, 1-norokadaone, had no effect at any concentration. Calyculin A also caused a selective loss of Glu-MTs but was effective at 10 nM, consistent with Its more potent inhibition of PP1. That the loss of Glu-MTs reflected the loss of stable MTs from the cells was shown by the absence ofnocodazole-resistant MTs in OA-treated cells. OA did not appear to actvate a MT-severing activity, since no MT frments were observed after OA treatment of cels pretreated with taxol. These results suggest that PP1 and perhaps PP2A are involved in the regulaton of MT stability in cells and show that the dynamic and stable subsets of MTs are regulated differentially by protein phosphorylation.Microtubules (MTs), a major component of the cytoskeleton, have been shown to be involved in the establishment of cell morphology, motility and differentiation (reviewed in refs. 1 and 2). A role in these events inherently presupposes that MTs exhibit a certain degree of stability, yet studies have indicated that MTs are highly dynamic structures: in proliferating fibroblasts and epithelial cells in culture, the average half-life of MTs is about 5-10 min (3-6). For a typical fibroblast or epithelial cell, this turnover rate implies that the entire array of interphase MTs is replaced every hour. Despite the rapid turnover ofthe bulk of the MT array in vivo, a small subset of MTs exhibits significantly slower rates of turnover. The halflife of these "stable" MTs appears to be >1 hr (5, 7). In fact, Webster et aL (7) found that a significant number of MTs in each cell persisted for 16 hr, or virtually the entire interphase portion of the cell cycle. These studies argue that although most MTs are highly dynamic, a small subset of MTs are removed from this dynamic pool and are stabilized.

show abstract

“…In tissue cells, it has been difficult to establish cause and effect between Glu tubulin and microtubule stability. It has been inferred that stable microtubules are detyrosinated, because inhibiting the tubulin-tyrosine ligase did not alter the global dynamics of microtubules (9). The studies in yeast indicate that indeed incorporation of Glu tubulin into the lattice dictates microtubule stability.…”

Section: Microtubule Stability In Cells Expressingmentioning

confidence: 99%

“…A carboxypeptidase catalyzes the cyclic removal of tyrosine from tubulin and tubulintyrosine ligase can reattach tyrosine in a tRNA-independent reaction. The early studies in this area indicated that detyrosination itself does not confer stability unto the microtubule polymer (9). However, it was difficult to distinguish whether the modification dictated stability, or whether stabilized microtubules become modified.…”

Section: Microtubule Structurementioning

confidence: 99%

Microtubule composition: Cryptography of dynamic polymers

Bloom

2004

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Detyrosination of alpha tubulin does not stabilize microtubules in vivo [published erratum appears in J Cell Biol 1990 Sep;111(3):1325-6]

Cited by 141 publications

References 56 publications

Alteration of the C-terminal Amino Acid of Tubulin Specifically Inhibits Myogenic Differentiation

Alteration of the C-terminal Amino Acid of Tubulin Specifically Inhibits Myogenic Differentiation

Protein phosphatase inhibitors induce the selective breakdown of stable microtubules in fibroblasts and epithelial cells.

Microtubule composition: Cryptography of dynamic polymers

Contact Info

Product

Resources

About