MYBBP1A suppresses breast cancer tumorigenesis by enhancing the p53 dependent anoikis

Akaogi, Kensuke; Ono, Wakana; Hayashi, Yoshihiko; Kishimoto, Hiroyuki; Yanagisawa, Junn

doi:10.1186/1471-2407-13-65

Cited by 28 publications

(28 citation statements)

References 45 publications

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“…1B) and anti-p53 co-IP-s (data not shown). It was previously reported, that MYBBP1A physically interacts with p53 [1]. The interaction of MYBBP1A with CDK2 was further confirmed by co-IP of MYBBP1A with anti-CDK2 antibody using nuclear extract prepared from HEK293 cells overexpressing highact TPPII (Fig.…”

Section: Resultssupporting

confidence: 64%

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TPPII, MYBBP1A and CDK2 form a protein–protein interaction network

Nahálková¹,

Tomkinson²

2014

Archives of Biochemistry and Biophysics

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Section: Resultssupporting

confidence: 64%

“…p21 [1] p21F primer: 5 0 -GGAGACTCTCAGGGTCGAAA-3 0 and p21R primer: 5 0 -TTAGGGCTTCCTCTTGGAGA-3 0 (200 nM each); 95°C for 2 min, 40 cycles of 10 s at 95°C and 15 s at 57°C.…”

Section: Mybbp1a [27]mentioning

confidence: 99%

TPPII, MYBBP1A and CDK2 form a protein–protein interaction network

Nahálková¹,

Tomkinson²

2014

Archives of Biochemistry and Biophysics

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“…TPPII functions downstream of the UPS and it may fulfill double role in the proteolysis and in other cellular functions mediated through protein-protein interactions. The p53 regulation on the transcription level may also be affected through the interaction of TPPII with MYBBP1A [13], which binds to p53 and enhances its transcription [28]. The present study confirmed interactions of TPPII with p53 both in the cytoplasmic and the nuclear subcellular compartments.…”

Section: Discussionsupporting

confidence: 81%

“…On the cellular level, the model mice showed functional links between TPPII, p53, and NF-jB [8] presented by increasing of p53 expression and the level of NF-jB in T-cells and by decreasing of NF-jB in fibroblasts. The transcription factor NFjB was found to be co-repressed by MYBBP1A [32], which directly interacted with both TPPII and p53 via protein-protein interactions [13,28]. Interestingly, MYBBP1A inhibited apoptosis through an activation of several antiapoptotic factors e.g.…”

Section: Discussionmentioning

confidence: 99%

Novel protein–protein interactions of TPPII, p53, and SIRT7

Nahálková

2015

Mol Cell Biochem

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Novel protein-protein interactions of TPPII, SIRT7, and p53 were detected by co-immunoprecipitation using both HeLa cell lysates and the cytoplasmic fraction prepared by fractionation of mouse liver tissue. The interactions were further verified in vivo by in situ proximity ligation assay (PLA) within control HEK293 cells transformed with empty vector, highactTPPII HEK293 cells over-expressing murine TPPII displaying high specific enzymatic activity and in lowactTPPII HEK293 cells over-expressing human TPPII having low specific activity of the enzyme. Besides an abundant cytoplasmic localization of TPPII-p53 interaction signal, the nuclear interactions were also demonstrated. The cytoplasmic interactions were likewise detected between TPPII and SIRT7 in control HEK293 and lowactTPPII HEK293 cells. The interactions of SIRT7 with p53 were confirmed in three HEK293 cell transformants as well. The cytoplasmic occurrence of SIRT7 protein was demonstrated by immunofluorescence, when both nucleolar and cytoplasmic signals were identified within HEK293 cells and primary human fibroblasts. The unique cytoplasmic localization of SIRT7 protein was discussed based on an epitope specificity of N-terminus specific SIRT7 antibodies utilized in the present study compared with C-terminus specific antibodies previously used for nuclear detection of SIRT7 by other authors. The epitope sequence of N-terminal antibodies is occurring in all three splicing variants of SIRT7 compared to the epitope of C-terminal antibody, which is specific exclusively to the splicing variant 1. The cytoplasmic localization of p53 detected by immunofluorescence supported the results from its interactions with TPPII and SIRT7 observed by in situ PLA within model cells. Novel interactions of TPPII, p53, and SIRT7 presented in this study might contribute to the knowledge of the regulatory effects of these proteins on apoptotic pathways and to the understanding mechanisms of aging and lifespan regulation.

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“…MYBBP1A can bind to p53 and enhance the transcription of p53 target genes (35,36), and its inhibition significantly enhanced tumorigenesis (35). MYBBP1A can also interact with NF-kB and inhibit NF-kB-dependent transcription (36).…”

Section: Discussionmentioning

confidence: 99%

Therapeutic Effects of XPO1 Inhibition in Thymic Epithelial Tumors

Conforti¹,

Zhang²,

Rao³

et al. 2017

Cancer Res

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Exportin 1 (XPO1) mediates nuclear export of many cellular factors known to play critical roles in malignant processes, and selinexor (KPT-330) is the first XPO1-selective inhibitor of nuclear export compound in advanced clinical development phase for cancer treatment. We demonstrated here that inhibition of XPO1 drives nuclear accumulation of important cargo tumor suppressor proteins, including transcription factor FOXO3a and p53 in thymic epithelial tumor (TET) cells, and induces p53-dependent and -independent antitumor activity in vitro. Selinexor suppressed the growth of TET xenograft tumors in athymic nude mice via inhibition of cell proliferation and induction of apoptosis. Loss of p53 activity or amplification of XPO1 may contribute to resistance to XPO1 inhibitor in TET. Using mass spectrometry-based proteomics analysis, we identified a number of proteins whose abundances in the nucleus and cytoplasm shifted significantly following selinexor treatment in the TET cells. Furthermore, we found that XPO1 was highly expressed in aggressive histotypes and advanced stages of human TET, and high XPO1 expression was associated with poorer patient survival. These results underscore an important role of XPO1 in the pathogenesis of TET and support clinical development of the XPO1 inhibitor for the treatment of patients with this type of tumors. Cancer Res; 77(20); 5614-27. Ó2017 AACR.

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MYBBP1A suppresses breast cancer tumorigenesis by enhancing the p53 dependent anoikis

Cited by 28 publications

References 45 publications

TPPII, MYBBP1A and CDK2 form a protein–protein interaction network

TPPII, MYBBP1A and CDK2 form a protein–protein interaction network

Novel protein–protein interactions of TPPII, p53, and SIRT7

Therapeutic Effects of XPO1 Inhibition in Thymic Epithelial Tumors

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