Polo-like kinase 1-mediated phosphorylation of the GTP-binding protein Ran is important for bipolar spindle formation

Yang Feng; Jin Hui Yuan; Sharon C. Maloid; Rebecca Fisher; Terry D. Copeland; Dan L. Longo; Thomas P. Conrads; Timothy D. Veenstra; Andrea Ferris; Steve Hughes; Dimiter S. Dimitrov; Douglass K. Ferris

doi:10.1016/j.bbrc.2006.08.028

Polo-like kinase 1-mediated phosphorylation of the GTP-binding protein Ran is important for bipolar spindle formation

Yang Feng^*, Jin Hui Yuan, Sharon C. Maloid, Rebecca Fisher, Terry D. Copeland, Dan L. Longo, Thomas P. Conrads, Timothy D. Veenstra, Andrea Ferris, Steve Hughes, Dimiter S. Dimitrov, Douglass K. Ferris

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

14 Scopus citations

Abstract

Polo-like kinase functions are essential for the establishment of a normal bipolar mitotic spindle, although precisely how Plk1 regulates the spindle is uncertain. In this study, we report that the small GTP/GDP-binding protein Ran is associated with Plk1. Plk1 is capable of phosphorylating co-immunoprecipitated Ran in vitro on serine-135 and Ran is phosphorylated in vivo at the same site during mitosis when Plk1 is normally activated. Cell cultures over-expressing a Ran S135D mutant have significantly higher numbers of abnormal mitotic cells than those over-expressing either wild-type or S135A Ran. The abnormalities in S135D mutant cells are similar to cells over-expressing Plk1. Our data suggests that Ran is a physiological substrate of Plk1 and that Plk1 regulates the spindle organization partially through its phosphorylation on Ran.

Original language	English
Pages (from-to)	144-152
Number of pages	9
Journal	Biochemical and Biophysical Research Communications
Volume	349
Issue number	1
DOIs	https://doi.org/10.1016/j.bbrc.2006.08.028
State	Published - 13 Oct 2006
Externally published	Yes

Keywords

Cytokinesis
GTP-binding proteins
Mitosis
Plk1
Polo-like kinases
Ran

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10.1016/j.bbrc.2006.08.028

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Feng, Y., Yuan, J. H., Maloid, S. C., Fisher, R., Copeland, T. D., Longo, D. L., Conrads, T. P., Veenstra, T. D., Ferris, A., Hughes, S., Dimitrov, D. S., & Ferris, D. K. (2006). Polo-like kinase 1-mediated phosphorylation of the GTP-binding protein Ran is important for bipolar spindle formation. Biochemical and Biophysical Research Communications, 349(1), 144-152. https://doi.org/10.1016/j.bbrc.2006.08.028

@article{a0b9c920f06742d6a2bae4a7fbd5d894,

title = "Polo-like kinase 1-mediated phosphorylation of the GTP-binding protein Ran is important for bipolar spindle formation",

abstract = "Polo-like kinase functions are essential for the establishment of a normal bipolar mitotic spindle, although precisely how Plk1 regulates the spindle is uncertain. In this study, we report that the small GTP/GDP-binding protein Ran is associated with Plk1. Plk1 is capable of phosphorylating co-immunoprecipitated Ran in vitro on serine-135 and Ran is phosphorylated in vivo at the same site during mitosis when Plk1 is normally activated. Cell cultures over-expressing a Ran S135D mutant have significantly higher numbers of abnormal mitotic cells than those over-expressing either wild-type or S135A Ran. The abnormalities in S135D mutant cells are similar to cells over-expressing Plk1. Our data suggests that Ran is a physiological substrate of Plk1 and that Plk1 regulates the spindle organization partially through its phosphorylation on Ran.",

keywords = "Cytokinesis, GTP-binding proteins, Mitosis, Plk1, Polo-like kinases, Ran",

author = "Yang Feng and Yuan, {Jin Hui} and Maloid, {Sharon C.} and Rebecca Fisher and Copeland, {Terry D.} and Longo, {Dan L.} and Conrads, {Thomas P.} and Veenstra, {Timothy D.} and Andrea Ferris and Steve Hughes and Dimitrov, {Dimiter S.} and Ferris, {Douglass K.}",

note = "Funding Information: This publication has been funded in whole or in part with Federal funds from the National Cancer Institute, National Institutes of Health, under Contract No. NO1-CO-12400. The content of this publication does not necessarily reflect the views or policies of the Department of Health and Human Services, nor does mention of trade names, commercial products, or organizations imply endorsement by the US Government. Funding Information: This research was supported [in part] by the Intramural Research Program of the NIH, National Cancer Institute, Center for Cancer Research. ",

year = "2006",

month = oct,

day = "13",

doi = "10.1016/j.bbrc.2006.08.028",

language = "English",

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journal = "Biochemical and Biophysical Research Communications",

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Feng, Y, Yuan, JH, Maloid, SC, Fisher, R, Copeland, TD, Longo, DL, Conrads, TP, Veenstra, TD, Ferris, A, Hughes, S, Dimitrov, DS & Ferris, DK 2006, 'Polo-like kinase 1-mediated phosphorylation of the GTP-binding protein Ran is important for bipolar spindle formation', Biochemical and Biophysical Research Communications, vol. 349, no. 1, pp. 144-152. https://doi.org/10.1016/j.bbrc.2006.08.028

TY - JOUR

T1 - Polo-like kinase 1-mediated phosphorylation of the GTP-binding protein Ran is important for bipolar spindle formation

AU - Feng, Yang

AU - Yuan, Jin Hui

AU - Maloid, Sharon C.

AU - Fisher, Rebecca

AU - Copeland, Terry D.

AU - Longo, Dan L.

AU - Conrads, Thomas P.

AU - Veenstra, Timothy D.

AU - Ferris, Andrea

AU - Hughes, Steve

AU - Dimitrov, Dimiter S.

AU - Ferris, Douglass K.

N1 - Funding Information: This publication has been funded in whole or in part with Federal funds from the National Cancer Institute, National Institutes of Health, under Contract No. NO1-CO-12400. The content of this publication does not necessarily reflect the views or policies of the Department of Health and Human Services, nor does mention of trade names, commercial products, or organizations imply endorsement by the US Government. Funding Information: This research was supported [in part] by the Intramural Research Program of the NIH, National Cancer Institute, Center for Cancer Research.

PY - 2006/10/13

Y1 - 2006/10/13

N2 - Polo-like kinase functions are essential for the establishment of a normal bipolar mitotic spindle, although precisely how Plk1 regulates the spindle is uncertain. In this study, we report that the small GTP/GDP-binding protein Ran is associated with Plk1. Plk1 is capable of phosphorylating co-immunoprecipitated Ran in vitro on serine-135 and Ran is phosphorylated in vivo at the same site during mitosis when Plk1 is normally activated. Cell cultures over-expressing a Ran S135D mutant have significantly higher numbers of abnormal mitotic cells than those over-expressing either wild-type or S135A Ran. The abnormalities in S135D mutant cells are similar to cells over-expressing Plk1. Our data suggests that Ran is a physiological substrate of Plk1 and that Plk1 regulates the spindle organization partially through its phosphorylation on Ran.

AB - Polo-like kinase functions are essential for the establishment of a normal bipolar mitotic spindle, although precisely how Plk1 regulates the spindle is uncertain. In this study, we report that the small GTP/GDP-binding protein Ran is associated with Plk1. Plk1 is capable of phosphorylating co-immunoprecipitated Ran in vitro on serine-135 and Ran is phosphorylated in vivo at the same site during mitosis when Plk1 is normally activated. Cell cultures over-expressing a Ran S135D mutant have significantly higher numbers of abnormal mitotic cells than those over-expressing either wild-type or S135A Ran. The abnormalities in S135D mutant cells are similar to cells over-expressing Plk1. Our data suggests that Ran is a physiological substrate of Plk1 and that Plk1 regulates the spindle organization partially through its phosphorylation on Ran.

KW - Cytokinesis

KW - GTP-binding proteins

KW - Mitosis

KW - Plk1

KW - Polo-like kinases

KW - Ran

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C2 - 16930555

AN - SCOPUS:33748310692

SN - 0006-291X

VL - 349

SP - 144

EP - 152

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 1

ER -

Polo-like kinase 1-mediated phosphorylation of the GTP-binding protein Ran is important for bipolar spindle formation

Abstract

Keywords

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