Plk1 regulates liver tumor cell death by phosphorylation of TAp63

Komatsu, Shojiro; Takenobu, Hisanori; Ozaki, Toshinori; Ando, Kiyohiro; Koida, Nami; Suenaga, Yusuke; Ichikawa, Tomoe; Hishiki, Tomoro; Chiba, Tetsuhiro; Iwama, Atsushi; Yoshida, Hideo; Ohnuma, Naomi; Nakagawara, Akira; Kamijo, Takehiko

doi:10.1038/onc.2009.216

Cited by 27 publications

(26 citation statements)

References 42 publications

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“…2) TAP63 overexpression prevented 15-PGDH depletion-mediated increase of cell proliferation, colony formation, and migration. These findings are noteworthy, given that TAP63 is a member of the p53 family and functions as a key tumor suppressor distinct from p53 to mediate various biological processes, including cell proliferation, differentiation, and apoptosis (35,38,(42)(43)(44)(45)(46)(47)(48)(49)(50).…”

Section: -Pgdh Cascade Interacts With Ppar-␥ Smad2/3 and Tap63mentioning

confidence: 99%

15-Hydroxyprostaglandin Dehydrogenase-derived 15-Keto-prostaglandin E2 Inhibits Cholangiocarcinoma Cell Growth through Interaction with Peroxisome Proliferator-activated Receptor-γ, SMAD2/3, and TAP63 Proteins

Han

2013

Journal of Biological Chemistry

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Section: -Pgdh Cascade Interacts With Ppar-␥ Smad2/3 and Tap63mentioning

confidence: 99%

15-Hydroxyprostaglandin Dehydrogenase-derived 15-Keto-prostaglandin E2 Inhibits Cholangiocarcinoma Cell Growth through Interaction with Peroxisome Proliferator-activated Receptor-γ, SMAD2/3, and TAP63 Proteins

Han

2013

Journal of Biological Chemistry

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“…In addition to the abovementioned kinases, Plk1 [59], p38 [60], GSK3 [35], and Raf1 [16] kinases may be also involved in proteasome-dependent degradation of p63.…”

Section: Kinases Involved In P63 Protein Degradationmentioning

confidence: 99%

Regulation of p63 Protein Stability via Ubiquitin-Proteasome Pathway

Xiao

2014

BioMed Research International

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The p53-related p63 gene encodes multiple protein isoforms, which are involved in a variety of biological activities. p63 protein stability is mainly regulated by the ubiquitin-dependent proteasomal degradation pathway. Several ubiquitin E3 ligases have been identified and some protein kinases as well as other kinds of proteins are involved in regulation of p63 protein stability. These regulators are responsive to diverse extracellular signaling, resulting in changes of the p63 protein levels and impacting different biological processes.

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“…Multiple phosphorylation sites have been identified within DNp63a and other TP63 isoforms [26][27][28][29] however, the underlying signaling pathways and functional consequences are known for only a subset of these modifications. In response to cisplatin, DNp63a is phosphorylated by c-Abl and this is required for cell viability [30].…”

Section: Introductionmentioning

confidence: 99%

Regulation of Mammary Stem Cell Quiescence via Post-Translational Modification of DeltaNp63alpha

DeCastro¹,

Cherukuri²,

DiRenzo³

2012

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Public reporting burden for this collection of information is estimated to average 1 hour per response, including the time for reviewing instructions, searching existing data sources, gathering and maintaining the data needed, and completing and reviewing this collection of information. Send comments regarding this burden estimate or any other aspect of this collection of information, including suggestions for reducing this burden to Department of Defense, Washington Headquarters Services, Directorate for Information Operations and Reports (0704-0188), 1215 Jefferson Davis Highway, Suite 1204, Arlington, VA 22202-4302. Respondents should be aware that notwithstanding any other provision of law, no person shall be subject to any penalty for failing to comply with a collection of information if it does not display a currently valid OMB control number. PLEASE DO NOT RETURN YOUR FORM TO THE ABOVE ADDRESS. REPORT DATE December 2012 REPORT TYPE Annual Summary DATES COVERED 15November2011-14November2012 TITLE AND SUBTITLE Regulation of Mammary Stem Cell Quiescence via Post-Translational 5a. CONTRACT NUMBERModification of DeltaNp63alpha. 5b. GRANT NUMBERW81XWH-11-1-0043 5c. PROGRAM ELEMENT NUMBER AUTHOR(S)Andrew. J DeCastro, B.S., Pratima Cherukuri, M.S., James DiRenzo, PhD.5d. PROJECT NUMBER 5e. TASK NUMBER E-Mail: Andrew.J.DeCastro@Dartmouth.edu 5f. WORK UNIT NUMBER PERFORMING ORGANIZATION NAME(S) AND ADDRESS(ES) AND ADDRESS(ES) PERFORMING ORGANIZATION REPORT NUMBERDartmouth College, Hanover, NH 03755 SPONSORING / MONITORING AGENCY NAME(S) AND ADDRESS(ES) 10. SPONSOR/MONITOR'S ACRONYM(S)U.S. Army Medical Research and Materiel Command Fort Detrick, Maryland 21702-5012 SPONSOR/MONITOR'S REPORT NUMBER(S) DISTRIBUTION / AVAILABILITY STATEMENTApproved for Public Release; Distribution Unlimited SUPPLEMENTARY NOTES ABSTRACTThis document is the Annual Summary Report on the training grant awarded to Andrew DeCastro entitled Regulation of Mammary Stem Cell Quiescence via Post-translational Modification of ∆NP63α. Here, we report our findings of the effects of TGFβ (previously validated as a kinase in our kinome screen) mediated phosphorylation of ∆NP63α on stem cell behavior and mitotic activity. Task 1 aims to determine the effects of wild-type, phospho-ablative and phospho-mimetic alleles of ∆NP63α phosphorylation on stem cell behavior in vitro. Thus far, we demonstrate that stem cell enriched populations, as indicated by ALDH1 activity, contain higher concentrations of ∆NP63α mRNA. In addition, we demonstrate that the anti-clonogenic effects of TGFβ are mediated through phosphorylation of ∆NP63α, which is rescued via ectopic expression of the phospho-ablative mutant ∆NP63α-AA. Task 2 aims to identify putative ∆NP63α-kinases and determine their role in mitotic activation. Here we further characterize TGFβ-mediated phosphorylation of ∆NP63α. We demonstrate that TGFβ phosphorylation of ∆NP63α is a destabilizing event, and dependent on the proteasomal degradation pathway. We also report a non-canonical pathway in which ALK5 (TGF...

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Plk1 regulates liver tumor cell death by phosphorylation of TAp63

Cited by 27 publications

References 42 publications

15-Hydroxyprostaglandin Dehydrogenase-derived 15-Keto-prostaglandin E2 Inhibits Cholangiocarcinoma Cell Growth through Interaction with Peroxisome Proliferator-activated Receptor-γ, SMAD2/3, and TAP63 Proteins

15-Hydroxyprostaglandin Dehydrogenase-derived 15-Keto-prostaglandin E2 Inhibits Cholangiocarcinoma Cell Growth through Interaction with Peroxisome Proliferator-activated Receptor-γ, SMAD2/3, and TAP63 Proteins

Regulation of p63 Protein Stability via Ubiquitin-Proteasome Pathway

Regulation of Mammary Stem Cell Quiescence via Post-Translational Modification of DeltaNp63alpha

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