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Characterization of the interaction ...

Towers, Russell.

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Characterization of the interaction between the chicken anaemia virus protein apoptin and the anaphase-promoting complex.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Characterization of the interaction between the chicken anaemia virus protein apoptin and the anaphase-promoting complex./
Author:	Towers, Russell.
Published:	Ann Arbor : ProQuest Dissertations & Theses, : 2011,
Description:	61 p.
Notes:	Source: Masters Abstracts International, Volume: 73-01.
Contained By:	Masters Abstracts International73-01.
Subject:	Cellular biology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=MR75014
ISBN:	9780494750148

Characterization of the interaction between the chicken anaemia virus protein apoptin and the anaphase-promoting complex.
Towers, Russell.

Characterization of the interaction between the chicken anaemia virus protein apoptin and the anaphase-promoting complex. - Ann Arbor : ProQuest Dissertations & Theses, 2011 - 61 p.

Source: Masters Abstracts International, Volume: 73-01.

Thesis (M.Sc.)--McGill University (Canada), 2011.

This item must not be sold to any third party vendors.

The Chicken anaemia virus protein apoptin is able to induce apoptosis specifically in human transformed cells independently of p53 through a mechanism that remains to be elucidated. Current evidence suggests that apoptin acts through inhibition of the anaphase-promoting complex/cyclosome (APC/C), an E3 ubiquitin ligase required for mitosis, by binding to the subunit APC1. In this study, apoptin was found to induce dissociation and degradation of the APC/C by associating with other subunits in addition to APC1 (APC2, APC3/Cdc27 and APC7). The APC1 binding location was localized to the C-terminus, which was found to be implicated in the association with APC3/Cdc27 and APC7. Residues of apoptin forming a possible IR domain were found to be required for APC/C interaction. However, apoptin was not able to bind the TPR motifs 4-9 of APC3/Cdc27, which are known to interact with the IR domain of APC/C co-activator Cdh1. These results contribute to the understanding of apoptin action in transformed cells, which once fully defined could be exploited in the creation of novel chemotherapeutics.

ISBN: 9780494750148Subjects--Topical Terms:

3172791
Cellular biology.

Characterization of the interaction between the chicken anaemia virus protein apoptin and the anaphase-promoting complex.
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245 1 0 $a Characterization of the interaction between the chicken anaemia virus protein apoptin and the anaphase-promoting complex.
260 1 $a Ann Arbor : $b ProQuest Dissertations & Theses, $c 2011
300 $a 61 p.
500 $a Source: Masters Abstracts International, Volume: 73-01.
500 $a Publisher info.: Dissertation/Thesis.
502 $a Thesis (M.Sc.)--McGill University (Canada), 2011.
506 $a This item must not be sold to any third party vendors.
506 $a This item must not be added to any third party search indexes.
520 $a The Chicken anaemia virus protein apoptin is able to induce apoptosis specifically in human transformed cells independently of p53 through a mechanism that remains to be elucidated. Current evidence suggests that apoptin acts through inhibition of the anaphase-promoting complex/cyclosome (APC/C), an E3 ubiquitin ligase required for mitosis, by binding to the subunit APC1. In this study, apoptin was found to induce dissociation and degradation of the APC/C by associating with other subunits in addition to APC1 (APC2, APC3/Cdc27 and APC7). The APC1 binding location was localized to the C-terminus, which was found to be implicated in the association with APC3/Cdc27 and APC7. Residues of apoptin forming a possible IR domain were found to be required for APC/C interaction. However, apoptin was not able to bind the TPR motifs 4-9 of APC3/Cdc27, which are known to interact with the IR domain of APC/C co-activator Cdh1. These results contribute to the understanding of apoptin action in transformed cells, which once fully defined could be exploited in the creation of novel chemotherapeutics.
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