Association of mitogen-activated protein kinases with microtubules in mouse macrophages.

Ding, Aihao; Chen, Bihua; Fuortes, Michele; Blum, Elissa

doi:10.1084/jem.183.4.1899

Cited by 39 publications

(19 citation statements)

References 56 publications

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“…These results are consistent with reports that microtubule anomalies cause a net increase in tyrosine phosphorylation (Bershadsky et al, 1996, Wolfson et al, 1997, but decreases also have been reported (Roberge et al, 1993). More recently, microtubule perturbations have been shown to activate the mitogen-activated protein kinase (MAPK) (Extracellular signal-regulated kinase, ERK) pathway (Ding et al, 1996, Yujiri et al, 1999, which suggests a possible mechanism for microtubule-associated apoptosis in non-neuronal cells. A panERK antibody (Transduction Laboratories), however, failed to Figure 4B and D).…”

Section: Tyrosine Phosphorylation Of a 90 Kda Proteinsupporting

confidence: 88%

Increased protein tyrosine phosphorylation in apoptotic neural cell death due to microtubule perturbations

Chromy

Lambert²,

Klein³

2000

neurotox res

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The microtubule-perturbing drugs colchicine and taxol have been found to induce apoptosis in a CNS neuronal cell line. Apoptosis in drug-treated rat B103 neuroblastoma cells was evident in characteristic morphological changes, internucleosomal DNA fragmentation, and loss of nuclear content. Since colchicine and taxol have opposite actions on microtubule integrity, disruption of the active turnover of the microtubule network appears to be a crucial step for apoptosis to occur. It has been suggested that the basis for apoptosis by these drugs derives from their known block of the cell cycle at G/M, but this does not appear the sole reason as both colchicine and taxol were able to evoke high levels of apoptosis in cells differentiated by BtcAMP or serum withdrawal. Further tests of cellular consequences of microtubule perturbation revealed a specific impact on signal transduction involving protein tyrosine phosphorylation. Immunoprecipitation with antibodies against tyrosine phosphorylated proteins showed a striking increase in the phosphorylation of a Triton-insoluble ~90 kDa protein, roughly concurrent with the onset of internucleosomal DNA fragmentation. Cycloheximide and genistein significantly reduced cell death and blocked appearance of the ~90 kDa tyrosine phosphorylated protein. Data suggest the hypothesis that signal transduction leading to apoptosis can be triggered by anomalous microtubule turnover and that the mechanism involves tyrosine phosphorylation of a ~90 kDa Triton-resistant protein.

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Section: Tyrosine Phosphorylation Of a 90 Kda Proteinsupporting

confidence: 88%

Increased protein tyrosine phosphorylation in apoptotic neural cell death due to microtubule perturbations

Chromy

Lambert²,

Klein³

2000

neurotox res

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show abstract

“…56,57 Microtubules are associated with serine/threonine kinases and phosphatases. [58][59][60][61] As the plasma membrane is an important source of signals during interphase, microtubules may be a principal location of signaling following mitotic arrest. Since mitochondria, an organelle where many members of the Bcl-2 family reside, 62 has proximity to microtubules, this may direct microtubule disruption to the apoptotic machinery.…”

Section: Discussionmentioning

confidence: 99%

Mitogen-activated protein kinase pathway is dispensable for microtubule-active drug-induced Raf-1/Bcl-2 phosphorylation and apoptosis in leukemia cells

Chuman

Bergan

et al. 1999

Leukemia

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Raf-1 activation and Bcl-2 hyperphosphorylation following treatment with paclitaxel (Taxol) or other microtubule-active drugs is associated with mitotic arrest. Here we show that microtubule-active drugs do not activate the mitogen-activated protein kinase (MAPK) pathway in leukemia cells. PD98059, a MEK inhibitor, and SB202190, a p38 MAP kinase inhibitor, do not abrogate Bcl-2 phosphorylation nor apoptosis. Simultaneously with PARP cleavage, paclitaxel induces cleavage of Bcl-2 protein yielding a potentially pro-apoptotic 22 kDa product. In comparison, the stimulation of Raf-1 by phorbol ester (TPA) activates the MAPK pathway, causes MAPK-dependent p21 WAF1/CIP1 induction, Rb dephosphorylation and growth arrest without Bcl-2 phosphorylation or apoptosis. Like TPA, cAMP induces p21 WAF1/CIP1 but does not cause Bcl-2 phosphorylation. MEKK1 and Ras, upstream activators of JNK and ERK MAPK, also fail to induce Bcl-2 hyperphosphorylation. Although Lck tyrosine kinase has been recently implicated in Raf-1 activation during mitotic arrest, microtubule-active drugs induce Raf-1/Bcl-2 hyperphosphorylation and apoptosis in a Lck-deficient Jurkat cells. Therefore, microtubule-active drugs induce apoptosis which is associated with Raf-1 and Bcl-2 phosphorylation and Bcl-2 cleavage but is independent of the MAPK pathway. In contrast, TPA-activated MAPK pathway causes p21 WAF1/CIP1 -dependent growth arrest without apoptosis.

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“…Microtubule damaging agents have been shown to activate MAPK without altering the level of MAPK expression (Ding et al, 1996;Wang et al, 1998;Shtil et al, 1999). We therefore investigated the effects of ATRA and docetaxel on MAPK activity.…”

Section: Effect Of Atra and Docetaxel On Activation Of Mapkmentioning

confidence: 99%

Modulation of docetaxel-induced apoptosis and cell cycle arrest by all- trans retinoic acid in prostate cancer cells

et al. 2001

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We report that all- trans retinoic acid (ATRA) enhanced the toxicity of docetaxel against DU145 and LNCaP prostate cancer cells, and that the nature of the interaction between ATRA and docetaxel was highly synergistic. Docetaxel-induced apoptotic cell death was associated with phosphorylation and hence inactivation of Bcl-2. ATRA enhanced docetaxel-induced apoptosis and combined treatment with ATRA and docetaxel resulted in down-regulation of Bcl-2. Docetaxel caused phosphorylation and hence inactivation of cdc2 kinase result ing in G2/M arrest. ATRA inhibited docetaxel-induced phosphorylation of cdc2 resulting in activation of cdc2 kinase and partial reversal of the G2/M arrest. ATRA also inhibited docetaxel-induced activation of MAPK indicating that the effects of docetaxel and ATRA on cdc2 phosphorylation are dependent on MAPK. We conclude that ATRA synergistically enhances docetaxel toxicity by down-regulating Bcl-2 expression and partially reverses the docetaxel-induced G2/M arrest by inhibiting docetaxel-induced cdc2 phosphorylation in a pathway that is dependent on MAPK. ¬© 2001 Cancer Research Campaign http://www.bjcancer.com

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Association of mitogen-activated protein kinases with microtubules in mouse macrophages.

Cited by 39 publications

References 56 publications

Increased protein tyrosine phosphorylation in apoptotic neural cell death due to microtubule perturbations

Increased protein tyrosine phosphorylation in apoptotic neural cell death due to microtubule perturbations

Mitogen-activated protein kinase pathway is dispensable for microtubule-active drug-induced Raf-1/Bcl-2 phosphorylation and apoptosis in leukemia cells

Modulation of docetaxel-induced apoptosis and cell cycle arrest by all- trans retinoic acid in prostate cancer cells

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