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Degradation of the human papillomavi...

Gonzalez-Razzetti, Sonia Lamar.

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Degradation of the human papillomavirus type 16 E7 oncoprotein and E7-mediated degradation of the retinoblastoma tumor suppressor.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Degradation of the human papillomavirus type 16 E7 oncoprotein and E7-mediated degradation of the retinoblastoma tumor suppressor./
Author:	Gonzalez-Razzetti, Sonia Lamar.
Description:	164 p.
Notes:	Adviser: Karl Munger.
Contained By:	Dissertation Abstracts International63-04B.
Subject:	Biology, Cell. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3051171
ISBN:	0493656774

Degradation of the human papillomavirus type 16 E7 oncoprotein and E7-mediated degradation of the retinoblastoma tumor suppressor.
Gonzalez-Razzetti, Sonia Lamar.

Degradation of the human papillomavirus type 16 E7 oncoprotein and E7-mediated degradation of the retinoblastoma tumor suppressor. - 164 p.

Adviser: Karl Munger.

Thesis (Ph.D.)--Harvard University, 2002.

The steady-state level and metabolic half-life of the retinoblastoma tumor suppressor protein, pRB, are decreased in cells that express high-risk human papillomavirus E7 proteins. My work shows that pRB degradation is a direct activity of E7 and does not reflect a property of cell lines acquired during the selection process for E7 expression. An amino terminal domain of E7 that does not directly contribute to pRB binding, but is required for transformation, is also necessary for E7-mediated pRB degradation. Treatment with inhibitors of the 26S proteasome not only blocks E7-mediated pRB degradation, but also causes stabilization of E7. Mutagenic analyses, however, reveal that proteasomal degradation of E7 and pRB are not linked processes. HPV-16 E7 also targets the pRB-related proteins, p107 and p130, for destabilization by a proteasome-dependent mechanism. Using the SAOS2 flat cell assay as a biological read-out for pRB function, I demonstrate that pRB degradation, not solely binding, is important for E7-induced inactivation of pRB. Lastly, I have begun characterization of a novel interaction between HPV-16 E7 and p62, a ubiquitin binding protein. Establishing the biological implications of this interaction may be key to understanding how HPV-16 E7 targets pRB for degradation.

ISBN: 0493656774Subjects--Topical Terms:

1017686
Biology, Cell.

Degradation of the human papillomavirus type 16 E7 oncoprotein and E7-mediated degradation of the retinoblastoma tumor suppressor.
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035 $a (UnM)AAI3051171
035 $a AAI3051171
040 $a UnM $c UnM
100 1 $a Gonzalez-Razzetti, Sonia Lamar. $3 1251314
245 1 0 $a Degradation of the human papillomavirus type 16 E7 oncoprotein and E7-mediated degradation of the retinoblastoma tumor suppressor.
300 $a 164 p.
500 $a Adviser: Karl Munger.
500 $a Source: Dissertation Abstracts International, Volume: 63-04, Section: B, page: 1647.
502 $a Thesis (Ph.D.)--Harvard University, 2002.
520 $a The steady-state level and metabolic half-life of the retinoblastoma tumor suppressor protein, pRB, are decreased in cells that express high-risk human papillomavirus E7 proteins. My work shows that pRB degradation is a direct activity of E7 and does not reflect a property of cell lines acquired during the selection process for E7 expression. An amino terminal domain of E7 that does not directly contribute to pRB binding, but is required for transformation, is also necessary for E7-mediated pRB degradation. Treatment with inhibitors of the 26S proteasome not only blocks E7-mediated pRB degradation, but also causes stabilization of E7. Mutagenic analyses, however, reveal that proteasomal degradation of E7 and pRB are not linked processes. HPV-16 E7 also targets the pRB-related proteins, p107 and p130, for destabilization by a proteasome-dependent mechanism. Using the SAOS2 flat cell assay as a biological read-out for pRB function, I demonstrate that pRB degradation, not solely binding, is important for E7-induced inactivation of pRB. Lastly, I have begun characterization of a novel interaction between HPV-16 E7 and p62, a ubiquitin binding protein. Establishing the biological implications of this interaction may be key to understanding how HPV-16 E7 targets pRB for degradation.
590 $a School code: 0084.
650 4 $a Biology, Cell. $3 1017686
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Health Sciences, Oncology. $3 1018566
690 $a 0307
690 $a 0379
690 $a 0992
710 2 0 $a Harvard University. $3 528741
773 0 $t Dissertation Abstracts International $g 63-04B.
790 $a 0084
790 1 0 $a Munger, Karl, $e advisor
791 $a Ph.D.
792 $a 2002
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3051171