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Modulator of apoptosis 1 (MOAP-1) is a tumor suppressor protein linked to the RASSF1A protein.

Law J, Salla M, Zare A, Wong Y, Luong L, Volodko N, Svystun O, Flood K, Lim J, Sung M, Dyck JR, Tan CT, Su YC, Yu VC, Mackey J, Baksh S - J. Biol. Chem. (2015)

Bottom Line: It is an integral partner to the tumor suppressor protein, Ras association domain family 1A (RASSF1A), and functions to activate the Bcl-2 family pro-apoptotic protein Bax.Although RASSF1A is now considered a bona fide tumor suppressor protein, the role of MOAP-1 as a tumor suppressor protein has yet to be determined.Overexpression of MOAP-1 in several cancer cell lines resulted in reduced tumorigenesis and up-regulation of genes involved in cancer regulatory pathways that include apoptosis (p53, Fas, and MST1), DNA damage control (poly(ADP)-ribose polymerase and ataxia telangiectasia mutated), those within the cell metabolism (IR-α, IR-β, and AMP-activated protein kinase), and a stabilizing effect on microtubules.

View Article: PubMed Central - PubMed

Affiliation: From the Departments of Biochemistry and.

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MOAP-1 can associate robustly with tubulin isoforms, may not require RASSF1A for this association, and can stabilize microtubules. Association of MOAP-1 with tubulin isoforms in SW40 cells (A), in H1299 cells (B), and in SW480 cells (C) used previously published mutants of MOAP-1 as indicated. D, acetylation status of α-tubulin−/+ Myc-MOAP-1 was determined with an anti-acetyl-α-tubulin antibody as indicated and quantified in the bottom panel. Bottom panel, total lysates of H1299 cells −/+ MOAP-1 or 1A were immunoblotted (IB) for acetylated tubulin followed by reprobing with an α-tubulin antibody to total tubulin content. Densitometry was carried on the immunoblots using the ImageJ software and plotted as shown. Expression of Myc-MOAP-1 and HA-1A was comparable (data not shown), and n = 3 for each point was independently carried out. IP, immunoprecipitation; WCL, whole cell lysate; Tx, treatment.
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Figure 9: MOAP-1 can associate robustly with tubulin isoforms, may not require RASSF1A for this association, and can stabilize microtubules. Association of MOAP-1 with tubulin isoforms in SW40 cells (A), in H1299 cells (B), and in SW480 cells (C) used previously published mutants of MOAP-1 as indicated. D, acetylation status of α-tubulin−/+ Myc-MOAP-1 was determined with an anti-acetyl-α-tubulin antibody as indicated and quantified in the bottom panel. Bottom panel, total lysates of H1299 cells −/+ MOAP-1 or 1A were immunoblotted (IB) for acetylated tubulin followed by reprobing with an α-tubulin antibody to total tubulin content. Densitometry was carried on the immunoblots using the ImageJ software and plotted as shown. Expression of Myc-MOAP-1 and HA-1A was comparable (data not shown), and n = 3 for each point was independently carried out. IP, immunoprecipitation; WCL, whole cell lysate; Tx, treatment.

Mentions: MOAP-1 can inhibit tumor formation driven by HCT116 colon cancer cells in vivo. HCT116 colon cancer cells with overexpressed proteins (A and B) or with shRNA to MOAP-1 (C) were generated by transient transfection with the indicated expression vectors. Cells were prepared and injected into nude mice as in Fig. 9. For HCT116 cells, the p value between vector and HA-RASSF1A and vector and Myc-MOAP-1 was 0.0026 and 0.0043, respectively; n = 10–16 for all. B, middle, expression of the indicated constructs are shown as well as mouse and tumor images, B, far right, representative tumors at day 35 of tumor growth. A, tumor images were captured using a multispectral FX instrument from Carestream to support the use of stable expression of GFP constructs for this assay. MOAP-1 shRNA in C results in >70% loss of MOAP-1 expression as presented.


Modulator of apoptosis 1 (MOAP-1) is a tumor suppressor protein linked to the RASSF1A protein.

Law J, Salla M, Zare A, Wong Y, Luong L, Volodko N, Svystun O, Flood K, Lim J, Sung M, Dyck JR, Tan CT, Su YC, Yu VC, Mackey J, Baksh S - J. Biol. Chem. (2015)

MOAP-1 can associate robustly with tubulin isoforms, may not require RASSF1A for this association, and can stabilize microtubules. Association of MOAP-1 with tubulin isoforms in SW40 cells (A), in H1299 cells (B), and in SW480 cells (C) used previously published mutants of MOAP-1 as indicated. D, acetylation status of α-tubulin−/+ Myc-MOAP-1 was determined with an anti-acetyl-α-tubulin antibody as indicated and quantified in the bottom panel. Bottom panel, total lysates of H1299 cells −/+ MOAP-1 or 1A were immunoblotted (IB) for acetylated tubulin followed by reprobing with an α-tubulin antibody to total tubulin content. Densitometry was carried on the immunoblots using the ImageJ software and plotted as shown. Expression of Myc-MOAP-1 and HA-1A was comparable (data not shown), and n = 3 for each point was independently carried out. IP, immunoprecipitation; WCL, whole cell lysate; Tx, treatment.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4591801&req=5

Figure 9: MOAP-1 can associate robustly with tubulin isoforms, may not require RASSF1A for this association, and can stabilize microtubules. Association of MOAP-1 with tubulin isoforms in SW40 cells (A), in H1299 cells (B), and in SW480 cells (C) used previously published mutants of MOAP-1 as indicated. D, acetylation status of α-tubulin−/+ Myc-MOAP-1 was determined with an anti-acetyl-α-tubulin antibody as indicated and quantified in the bottom panel. Bottom panel, total lysates of H1299 cells −/+ MOAP-1 or 1A were immunoblotted (IB) for acetylated tubulin followed by reprobing with an α-tubulin antibody to total tubulin content. Densitometry was carried on the immunoblots using the ImageJ software and plotted as shown. Expression of Myc-MOAP-1 and HA-1A was comparable (data not shown), and n = 3 for each point was independently carried out. IP, immunoprecipitation; WCL, whole cell lysate; Tx, treatment.
Mentions: MOAP-1 can inhibit tumor formation driven by HCT116 colon cancer cells in vivo. HCT116 colon cancer cells with overexpressed proteins (A and B) or with shRNA to MOAP-1 (C) were generated by transient transfection with the indicated expression vectors. Cells were prepared and injected into nude mice as in Fig. 9. For HCT116 cells, the p value between vector and HA-RASSF1A and vector and Myc-MOAP-1 was 0.0026 and 0.0043, respectively; n = 10–16 for all. B, middle, expression of the indicated constructs are shown as well as mouse and tumor images, B, far right, representative tumors at day 35 of tumor growth. A, tumor images were captured using a multispectral FX instrument from Carestream to support the use of stable expression of GFP constructs for this assay. MOAP-1 shRNA in C results in >70% loss of MOAP-1 expression as presented.

Bottom Line: It is an integral partner to the tumor suppressor protein, Ras association domain family 1A (RASSF1A), and functions to activate the Bcl-2 family pro-apoptotic protein Bax.Although RASSF1A is now considered a bona fide tumor suppressor protein, the role of MOAP-1 as a tumor suppressor protein has yet to be determined.Overexpression of MOAP-1 in several cancer cell lines resulted in reduced tumorigenesis and up-regulation of genes involved in cancer regulatory pathways that include apoptosis (p53, Fas, and MST1), DNA damage control (poly(ADP)-ribose polymerase and ataxia telangiectasia mutated), those within the cell metabolism (IR-α, IR-β, and AMP-activated protein kinase), and a stabilizing effect on microtubules.

View Article: PubMed Central - PubMed

Affiliation: From the Departments of Biochemistry and.

Show MeSH
Related in: MedlinePlus