Home Dartmouth Dissertations belden2001 1

Reference URL

To link to the entire object, paste this link in email, IM or document

To embed the entire object, paste this HTML in website

To link to this page, paste this link in email, IM or document

To embed this page, paste this HTML in website

Characterization of COPII vesicle proteins involved in sorting between the endoplasmic reticulum and golgi apparatus in Sacch[a]romyces cerevisiae.

you wish to report:

Your comment:

Your Name:

Submit

Cancel

...

Call No.	QH601 .B45 2001
Author	Belden, William J.
Title	Characterization of COPII vesicle proteins involved in sorting between the endoplasmic reticulum and golgi apparatus in Sacch[a]romyces cerevisiae.
Date	2001
Abstract	Intracellular transport between the ER and Golgi is mediated by vesicles that bud from donor membranes and then fuse with acceptor membranes. Bi-directional vesicle transport maintains distinct organelle composition through a process known as molecular sorting. Collectively, molecular sorting refers to the process of actively selecting or excluding proteins and lipids into transport vesicles. Some of the proteins involved in sorting have been identified although the mechanisms remain obscure. This dissertation examines proteins contained on ER-derived vesicles (Ervs) and how these proteins facilitate sorting. Erv function requires bi-directional ER to Golgi transport therefore it was determined how the cytoplamic tail sequences of Emp24p and Erv25p function in transport. Both Emp24p and Erv25p tail sequences are sufficient to direct anterograde transport and interact with COPII subunits, however the Erv25p tail is necessary to direct retrograde transport. A vexing question regarding p24 function is why the deletion strains secrete ER chaperones to the cell culture supernatant. A comprehensive analysis indicates that p24 proteins have an activated UPR and this results in saturation of the HDEL retrieval mechanism leading to secretion of ER chaperones. Another vesicle protein, Erv29p, functions as a classical membrane bound cargo receptor that is required for efficient transport of the secretory cargo glycosylated pro-α-factor. Further analysis of the p24 deletion and erv29Δ strains indicates that both have an activated UPR but only p24 deletions secrete HDEL proteins. This observation provides further clues into the mechanisms of p24 function. The collective data presented in this dissertation demonstrate that molecular sorting involves active selection, retention and retrieval mechanism.
Description	1 online resource (119 leaves) : illustrations
Format	application/pdf
Advisor	Barlowe, Charles
Subject	Membrane proteins -- Physiological transport. ; Carrier proteins. ; Biological transport -- Regulation. ; Saccharomyces cerevisiae -- Cytology. ; Golgi apparatus. ; Endoplasmic reticulum.
College	Dartmouth Medical School -- Department of Biochemistry.
Issuing Body	Dartmouth Dissertations are made available through the Dartmouth Digital Library.
Degree	Thesis (Ph.D)--Dartmouth College.
Copyright	In Copyright. This material is protected by copyright and/or related rights. You are free to use this material in any way that is permitted by copyright law that applies to your use. For other uses, you need to obtain permission from the rights-holder(s). http://rightsstatements.org/page/InC/1.0/
DOI	https://doi.org/10.1349/ddlp.2966

Find results with:

Searching collections:

Home Dartmouth Dissertations belden2001 1

Characterization of COPII vesicle proteins involved in sorting between the endoplasmic reticulum and golgi apparatus in Sacch[a]romyces cerevisiae.

Object Description

Description

Characterization of COPII vesicle proteins involved in...

Characterization of COPII vesicle proteins involved in...

	All
	Pages Enter page numbers or page ranges separated by commas. For example: 1,3,5-12