Microtubule binding of the <i>Drosophila</i> DMAP‐85 protein is regulated by phosphorylation in vitro

Cambiazo, Verónica; Logarinho, Elsa; Pottstock, Hans; Sunkel, Cláudio E.

doi:10.1016/s0014-5793(00)02077-9

Cited by 9 publications

(6 citation statements)

References 60 publications

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“…Recent studies have indicated that the phosphorylation of microtubule-associated proteins plays a critical role in the regulation of microtubule stability (2,5). Several Drosophila pro-…”

Section: Discussionmentioning

confidence: 99%

“…Parental A549 cells were processed and analyzed in the same manner as a control. (2,5). Given that both Asp and DMAP-85 associate also with centrosomes or microtubules and that their interactions are regulated by phosphorylation (2,5) it is tempting to speculate that these human homologues are potential in vivo targets of Plk3.…”

Section: Fig 8 Apoptosis Induced By Plk3-a and Plk3mentioning

confidence: 99%

“…(2,5). Given that both Asp and DMAP-85 associate also with centrosomes or microtubules and that their interactions are regulated by phosphorylation (2,5) it is tempting to speculate that these human homologues are potential in vivo targets of Plk3. Centrosome abnormalities are implicated in chromosomal instability and in the development of cancer, and in fact, many cancer cells display multiple centrosomes or enhanced centrosomal activity (20).…”

Section: Fig 8 Apoptosis Induced By Plk3-a and Plk3mentioning

confidence: 99%

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Cell Cycle Arrest and Apoptosis Induced by Human Polo-Like Kinase 3 Is Mediated through Perturbation of Microtubule Integrity

Wang

Xie

Chen

et al. 2002

Molecular and Cellular Biology

125

123

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). Here we report that in most interphase cells endogenous Plk3 was predominantly localized around the nuclear membrane. Double labeling with Plk3 and ␥-tubulin, the latter a major component of pericentriole materials, revealed that Plk3 was closely associated with centrosomes and that its localization to centrosomes was dependent on the integrity of microtubules. Throughout mitosis, Plk3 appeared to be localized to mitotic apparatus such as spindle poles and mitotic spindles. During telophase, a significant amount of Plk3 was also detected in the midbody. Ectopic expression of Plk3 mutants dramatically changed cell morphology primarily due to their effects on microtubule dynamics. Expression of a constitutively active Plk3 (Plk3-A) resulted in rapid cell shrinkage, which led to formation of cells with an elongated, unsevered, and taxol-sensitive midbody. In contrast, cells expressing a kinase-defective Plk3 (Plk3 K52R ) mutant exhibited extended, deformed cytoplasmic structures, the phenotype of which was somewhat refractory to taxol treatment. Expression of both Plk3-A and Plk3 K52R induced apparent G 2 /M arrest followed by apoptosis, although the kinase-defective mutant was less effective. Taken together, our studies strongly suggest that Plk3 plays an important role in the regulation of microtubule dynamics and centrosomal function in the cell and that deregulated expression of Plk3 results in cell cycle arrest and apoptosis.

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“…Recent studies have indicated that the phosphorylation of microtubule-associated proteins plays a critical role in the regulation of microtubule stability (2,5). Several Drosophila pro-…”

Section: Discussionmentioning

confidence: 99%

Section: Fig 8 Apoptosis Induced By Plk3-a and Plk3mentioning

confidence: 99%

Section: Fig 8 Apoptosis Induced By Plk3-a and Plk3mentioning

confidence: 99%

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Cell Cycle Arrest and Apoptosis Induced by Human Polo-Like Kinase 3 Is Mediated through Perturbation of Microtubule Integrity

Wang

Xie

Chen

et al. 2002

Molecular and Cellular Biology

125

123

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“…Genetic evidence of the synergy of the polo 1 asp E3 double-mutant phenotype, as well as recent biochemical evidence, supports a role of polo in regulating centrosomal function through asp (23,34,68). Phosphorylation of DMAP-85 by polo was later shown to regulate its in vitro microtubule-binding activity (16). In addition, work with Xenopus egg extracts has suggested that Plx1 can phosphorylate the MAP Op18 and regulate its destabilizing activity (14).…”

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confidence: 87%

Plk Phosphorylation Regulates the Microtubule-Stabilizing Protein TCTP

Yarm

2002

Molecular and Cellular Biology

234

204

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The mitotic polo-like kinases have been implicated in the formation and function of bipolar spindles on the basis of their respective localizations and mutant phenotypes. To date, this putative regulation has been limited to a kinesin-like motor protein, a centrosomal structural protein, and two microtubule-associated proteins (MAPs). In this study, another spindle-regulating protein, the mammalian non-MAP microtubule-binding and -stabilizing protein, the translationally controlled tumor protein (TCTP), was identified as a putative Plk-interacting clone by a two-hybrid screen. Plk phosphorylates TCTP on two serine residues in vitro and cofractionates with the majority of kinase activity toward TCTP in mitotic cell lysates. In addition, these sites were demonstrated to be phosphorylated in vivo. Overexpression of a Plk phosphorylation site-deficient mutant of TCTP induced a dramatic increase in the number of multinucleate cells, rounded cells with condensed ball-like nuclei, and cells undergoing cell death, similar to both the reported anti-Plk antibody microinjection and the low-concentration taxol treatment phenotypes. These results suggest that phosphorylation decreases the microtubule-stabilizing activity of TCTP and promotes the increase in microtubule dynamics that occurs after metaphase.

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“…These included b-tubulin and two proteins of 85 kDa and approximately 200 kDa. Subsequently, it appears that these last two proteins are likely to be an 85 kDa MT-associated protein released from MTs following phosphorylation by Polo (Cambiazo et al, 2000) and Asp, the product of the abnormal spindle gene (Saunders et al, 1997;Avides and Glover, 1999;Avides et al, 2001;see below).…”

Section: In the Right Place At The Right Timementioning

confidence: 99%

Polo kinase and progression through M phase in Drosophila: a perspective from the spindle poles

Glover

2005

Oncogene

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Genes for the mitotic kinases Polo and Aurora A were first identified in Drosophila through screens of maternal effect lethal mutations for defects in spindle pole behaviour. These enzymes have been shown to be highly conserved and required for multiple functions in mitosis. Polo is stabilized at the centrosome by association with Hsp90. It is required for centrosome maturation on Mphase entry in order to recruit the c-tubulin ring complex and activate the abnormal spindle protein, Asp. These events facilitate the nucleation of minus ends of microtubules at the centrosome. The localization of Polo at the kinetochore and the mid-zone of the central spindle together with the phenotypes of polo mutants point to functions at the metaphase to anaphase transition and in cytokinesis. The latter are mediated, at least in part, through the Pavarotti kinesin-like motor protein and its conserved counterparts in other metazoans.

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Microtubule binding of the Drosophila DMAP‐85 protein is regulated by phosphorylation in vitro

Cited by 9 publications

References 60 publications

Cell Cycle Arrest and Apoptosis Induced by Human Polo-Like Kinase 3 Is Mediated through Perturbation of Microtubule Integrity

Cell Cycle Arrest and Apoptosis Induced by Human Polo-Like Kinase 3 Is Mediated through Perturbation of Microtubule Integrity

Plk Phosphorylation Regulates the Microtubule-Stabilizing Protein TCTP

Polo kinase and progression through M phase in Drosophila: a perspective from the spindle poles

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