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Investigation of the molecular mechanisms of Erv26p-dependent protein sorting.

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Call No.	QP552.C34 B84 2009
Author	Bue, Catherine A.
Title	Investigation of the molecular mechanisms of Erv26p-dependent protein sorting.
Date	2009
Abstract	Studies of the secretory pathway have revealed a multitude of secretory proteins that depend on the coat protein complex II (COPII) for export from the endoplasmic reticulum (ER) in transport vesicles. Some secretory proteins require protein sorting adaptors to provide an indirect link to the COPII coat. Protein sorting adaptors in ER-to-Golgi transport are generally thought to contain sorting signals that mediate binding to COPII as well as the retrograde-directed coatomer protein (COPI) coat for bi-directional trafficking between the ER and Golgi. However, mechanisms of protein sorting adaptor-dependent ER export remain unclear, including what fraction of secretory proteins require sorting adaptors, how many types of sorting adaptors are needed to accommodate the diversity of cargo, and the regulation of sorting adaptor-dependent transport. In this thesis, studies were performed on the uncharacterized S. cerevisiae ER vesicle protein known as Erv26p, and indicate that it is a novel protein sorting adaptor. Experimental evidence demonstrates that Erv26p is packaged efficiently into COPII vesicles, and strains lacking Erv26p show an ER accumulation of vacuolar pro-alkaline phosphatase (pro-ALP). pro-ALP interacts with Erv26p and is packaged into COPII vesicles in an Erv26p-dependent manner. To investigate the molecular mechanism of Erv26p-dependent sorting, mutations in conserved regions of Erv26p were made and analyzed. Erv26p interactions with both coat and cargo are required for efficient pro-ALP transport, and are independent of one another. Additionally, Erv26p homodimerization is important for pro-ALP interaction. The C-terminus of Erv26p is required for efficient COPII-dependent ER export, whereas the third luminal loop domain is involved in cargo recognition. These results have revealed mechanisms governing Erv26p-dependent transport, and future studies on this sorting adaptor-cargo pair should allow an elucidation of general mechanisms underlying receptor-mediated ER export.
Description	ix, 159 leaves : ill. (some col.) 28 cm.
Format	application/pdf
Advisor	Barlowe, Charles K., Wickner, William T., Higgs, Henry N., Miller, Elizabeth
Subject	Carrier proteins -- Molecular aspects. Membrane proteins -- Physiological transport. Proteins -- Secretion. Biological transport -- Regulation. Saccharomyces cerevisiae -- Molecular aspects. Endoplasmic reticulum. Golgi apparatus. Vesicular Transport Proteins. Protein Transport.
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	All rights reserved. No part of this book may be reproduced in any form by any electronic or mechanical means without permission in writing from the author.
DOI	http://dx.doi.org/10.1349/ddlp.259

Title	Page 1
Format	application/pdf
Issuing Body	Dartmouth Dissertations are made available through the Dartmouth Digital Library.
Degree	Thesis (Ph.D.)--Dartmouth College.
Full Text	Investigation of the Molecular Mechanisms of Erv26p-Dependent Protein Sorting A Thesis Submitted to the Faculty In partial fulfillment of the requirements for the Degree of Doctor of Philosophy in Biochemistry By Catherine A. Bue Dartmouth College Hanover, New Hampshire January 26, 2009 Examining Committee: ___________________ Charles Barlowe ___________________ William Wickner ___________________ Henry Higgs ___________________ ___________________ Brian Pogue Elizabeth Miller Dean of Graduate Studies

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