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Misfolded protein degradation requir...

Caldwell, Sabrina R.

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Misfolded protein degradation requires ER-Golgi transport and the novel cargo receptor, Erv29.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Misfolded protein degradation requires ER-Golgi transport and the novel cargo receptor, Erv29./
Author:	Caldwell, Sabrina R.
Description:	113 p.
Notes:	Source: Dissertation Abstracts International, Volume: 65-01, Section: B, page: 0030.
Contained By:	Dissertation Abstracts International65-01B.
Subject:	Biology, Cell. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3118827

Misfolded protein degradation requires ER-Golgi transport and the novel cargo receptor, Erv29.
Caldwell, Sabrina R.

Misfolded protein degradation requires ER-Golgi transport and the novel cargo receptor, Erv29. - 113 p.

Source: Dissertation Abstracts International, Volume: 65-01, Section: B, page: 0030.

Thesis (Ph.D.)--University of Missouri - Kansas City, 2004.

Proteins destined for the secretory pathway are translated and translocated into the endoplasmic reticulum where they undergo folding, oligosaccharide additions, and/or assemble with other subunits prior to export from the endoplasmic reticulum to the Golgi apparatus. As the proteins traverse the Golgi stacks, they receive further modifications and are transported to their final destination, which may be the cell surface, endosome, or vacuole. It has been debated whether proteins exiting the endoplasmic reticulum leave by a "bulk flow" mechanism or through an active, selective process where certain proteins exit at a faster rate than others. Erv29p was identified as a transmembrane protein isolated from endoplasmic reticulum derived vesicles that is necessary for the export of a subset of secretory proteins (CPY and PrA) from the endoplasmic reticulum, Erv29p. Evidence for Erv29p as a cargo receptor is that it physically interacts with its cargo proteins and is saturable. Erv29p cycles between the endoplasmic reticulum and the Golgi apparatus and the amino acid sequence indicates that it possesses a dilysine retrieval motif that I demonstrate is necessary for its long half-life, proper subcellular distribution and its function.Subjects--Topical Terms:

1017686
Biology, Cell.

Misfolded protein degradation requires ER-Golgi transport and the novel cargo receptor, Erv29.
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040 $a UnM $c UnM
100 1 $a Caldwell, Sabrina R. $3 1952491
245 1 0 $a Misfolded protein degradation requires ER-Golgi transport and the novel cargo receptor, Erv29.
300 $a 113 p.
500 $a Source: Dissertation Abstracts International, Volume: 65-01, Section: B, page: 0030.
500 $a Adviser: Antony A. Cooper.
502 $a Thesis (Ph.D.)--University of Missouri - Kansas City, 2004.
520 $a Proteins destined for the secretory pathway are translated and translocated into the endoplasmic reticulum where they undergo folding, oligosaccharide additions, and/or assemble with other subunits prior to export from the endoplasmic reticulum to the Golgi apparatus. As the proteins traverse the Golgi stacks, they receive further modifications and are transported to their final destination, which may be the cell surface, endosome, or vacuole. It has been debated whether proteins exiting the endoplasmic reticulum leave by a "bulk flow" mechanism or through an active, selective process where certain proteins exit at a faster rate than others. Erv29p was identified as a transmembrane protein isolated from endoplasmic reticulum derived vesicles that is necessary for the export of a subset of secretory proteins (CPY and PrA) from the endoplasmic reticulum, Erv29p. Evidence for Erv29p as a cargo receptor is that it physically interacts with its cargo proteins and is saturable. Erv29p cycles between the endoplasmic reticulum and the Golgi apparatus and the amino acid sequence indicates that it possesses a dilysine retrieval motif that I demonstrate is necessary for its long half-life, proper subcellular distribution and its function.
520 $a The endoplasmic reticulum possesses a quality control that monitors the folding of proteins. If proteins are unable to fold correctly, the quality control targets them to be degraded via endoplasmic reticulum associated degradation. Some components of this system are known, the majority of which are endoplasmic reticulum resident proteins. I demonstrate that some misfolded proteins transit beyond the endoplasmic reticulum prior to retrotranslocation and instead are reliant on the cargo receptor, Erv29p. Erv29p is necessary for the degradation of the misfolded proteins, CPY* and PrA*. Further investigations reveal that misfolded proteins travel to the Golgi apparatus where they may be modified prior to degradation. The misfolded proteins CPY* localizes with Golgi marker proteins when retrograde transport from the Golgi is blocked. The accumulation of CPY* in the Golgi redistributes to the endoplasmic reticulum upon relief of the retrograde block. Therefore, some misfolded proteins cycle between the ER-Golgi apparatus prior to degradation by the proteasome.
590 $a School code: 0134.
650 4 $a Biology, Cell. $3 1017686
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Biophysics, General. $3 1019105
690 $a 0379
690 $a 0307
690 $a 0786
710 2 0 $a University of Missouri - Kansas City. $3 1021712
773 0 $t Dissertation Abstracts International $g 65-01B.
790 1 0 $a Cooper, Antony A., $e advisor
790 $a 0134
791 $a Ph.D.
792 $a 2004
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3118827