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Conference Paper: PLK-1 interacts with RASSF1C and regulates its expression by a phosphorylation dependent mechanism

TitlePLK-1 interacts with RASSF1C and regulates its expression by a phosphorylation dependent mechanism
Authors
Issue Date2007
PublisherAmerican Association for Cancer Research
Citation
The 98th AACR Annual Meeting, Los Angeles, CA, 14-18 April 2007. In Cancer Research, 2007, v. 67 n. 9S, p. 5197 How to Cite?
AbstractPolo-like kinase-1 (Plk1) belongs to the polo-like kinase protein family which regulates mitotic progression and its activities was recently showed to be regulated by progressive phosphorylation at Ser137 and Thr210 during the cell cycle. One of its major roles during mitosis is to promote the mitotic spindle formation through direct interaction and phosphorylation of proteins involved in microtubule organization and assembly. Here, we report that Plk1 interacts with the 1C isoform of the RASSF1 protein family. RASSF1C, like RASSF1A, was recently showed to bind to and regulate microtubule stability. Although ectopic expression of the wild-type Plk1 failed to affect the expression of RASSF1C, the dominant active Plk1 mutants (T210D or S137D) significantly downregulated RASSF1C protein level. Meanwhile, a further downregulation of the RASSF1C protein was observed when a double mutant (T210D+S137D) was expressed, suggesting that the effect of Plk1 on RASSF1C depends on the kinase activities of Plk1. Interestingly, while Plk1 can also interact with RASSF1A, expression of either the wild-type or dominant active mutants did not affect the RASSF1A protein level. Taken together, our result demonstrated the microtubule regulator RASSF1C as a novel target of Plk1.
Persistent Identifierhttp://hdl.handle.net/10722/95753
ISSN
2015 Impact Factor: 8.556
2015 SCImago Journal Rankings: 5.372

 

DC FieldValueLanguage
dc.contributor.authorLing, MTen_HK
dc.contributor.authorFung, KLen_HK
dc.contributor.authorWang, Xen_HK
dc.contributor.authorWong, YCen_HK
dc.date.accessioned2010-09-25T16:12:10Z-
dc.date.available2010-09-25T16:12:10Z-
dc.date.issued2007en_HK
dc.identifier.citationThe 98th AACR Annual Meeting, Los Angeles, CA, 14-18 April 2007. In Cancer Research, 2007, v. 67 n. 9S, p. 5197en_HK
dc.identifier.issn0008-5472-
dc.identifier.urihttp://hdl.handle.net/10722/95753-
dc.description.abstractPolo-like kinase-1 (Plk1) belongs to the polo-like kinase protein family which regulates mitotic progression and its activities was recently showed to be regulated by progressive phosphorylation at Ser137 and Thr210 during the cell cycle. One of its major roles during mitosis is to promote the mitotic spindle formation through direct interaction and phosphorylation of proteins involved in microtubule organization and assembly. Here, we report that Plk1 interacts with the 1C isoform of the RASSF1 protein family. RASSF1C, like RASSF1A, was recently showed to bind to and regulate microtubule stability. Although ectopic expression of the wild-type Plk1 failed to affect the expression of RASSF1C, the dominant active Plk1 mutants (T210D or S137D) significantly downregulated RASSF1C protein level. Meanwhile, a further downregulation of the RASSF1C protein was observed when a double mutant (T210D+S137D) was expressed, suggesting that the effect of Plk1 on RASSF1C depends on the kinase activities of Plk1. Interestingly, while Plk1 can also interact with RASSF1A, expression of either the wild-type or dominant active mutants did not affect the RASSF1A protein level. Taken together, our result demonstrated the microtubule regulator RASSF1C as a novel target of Plk1.-
dc.languageengen_HK
dc.publisherAmerican Association for Cancer Research-
dc.relation.ispartofCancer Researchen_HK
dc.titlePLK-1 interacts with RASSF1C and regulates its expression by a phosphorylation dependent mechanismen_HK
dc.typeConference_Paperen_HK
dc.identifier.emailLing, MT: patling@HKUCC.hku.hken_HK
dc.identifier.emailWong, YC: ycwong@hkucc.hku.hken_HK
dc.identifier.authorityLing, MT=rp00449en_HK
dc.identifier.authorityWong, YC=rp00316en_HK
dc.identifier.hkuros147355en_HK
dc.identifier.spage120en_HK

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