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Molecular analysis of novel ER membrane proteins important for homeostasis in Saccharomyces cerevisiae.

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Call No.	QP552.M44 W55 2009
Author	Wilson, Joshua D.
Title	Molecular analysis of novel ER membrane proteins important for homeostasis in Saccharomyces cerevisiae.
Date	2009
Abstract	Endoplasmic reticulum (ER) homeostasis requires the coordination of anabolic and catabolic activities. A primary function of the ER is the biosynthesis and export of secretory proteins and lipids. Anterograde transport of only properly folded and assembled proteins requires a quality control machinery which can sense and ameliorate aberrant protein species. An additional requisite of high fidelity anterograde transport is a system to eliminate polypeptides that repeatedly fail quality control, known as ER associated degradation (ERAD). The work presented in this dissertation provides evidence for novel Saccharomyces cerevisiae membrane proteins functioning in biosynthetic (Yet1p and Yet3p) and degradative (Sel1p/Ubx2p) pathways which contribute to ER homeostasis. Sel1p was found in nearly stoichiometric association with the AAA ATPase Cdc48p and its cofactor Npl4p. Cdc48p, in association with Npl4p and Ufd1p, is known to play a critical role in ERAD thus suggesting a role for Sel1? in this process. Indeed, sel1 ? mutant cells displayed attenuated turnover of two model ERAD substrates. Furthermore, ER microsomes isolated from sel1 ? mutant cells had less associated Cdc48p, suggesting that Sel1p function in ERAD may involve the recruitment of Cdc48p to the ER membrane. Yet1p and Yet3p are sequence homologs of the mammalian BAP29 and BAP31 proteins. Like BAP29 and BAP31, Yet1p and Yet3p were primarily localized to the ER and formed a heteromeric complex. This Yet1p-Yet3p complex was found in distinct associations with the ER translocation machinery and with Scs2p-Opi1p, a complex important for INO1 derepression, suggesting that Yet1p and Yet3p may function in both protein and lipid biosynthesis. Association of the Yet1p-Yet3p complex with Scs2p-Opi1p appears to be critical for INO1 derepression because cells harboring yet1 ? or yet3 ? mutations were defective for growth in the absence of inositol and were unable to properly derepress INO1. A model for Yet1p-Yet3p function in Scs2p mediated INO1 derepression is proposed.
Description	xi, 191 leaves : ill. (some col.) 28 cm.
Format	application/pdf
Advisor	Barlowe, Charles K., Wickner, William T., Myers, Lawrence C., Brickner, Jason H.
Subject	Membrane proteins -- Physiological transport. Biological transport -- Regulation. Proteins -- Biodegradation. Proteins -- Synthesis -- Regulation. Endoplasmic reticulum. Cellular control mechanisms. Saccharomyces cerevisiae -- Molecular aspects.
College	Dartmouth College -- 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.323

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	Molecular Analysis of Novel ER Membrane Proteins Important for Homeostasis in Saccharomyces cerevisiae A Thesis Submitted to the Faculty in partial fulfillment of the requirements for the degree of Doctor of Philosophy in Biochemistry by Joshua D. Wilson DARTMOUTH COLLEGE Hanover, New Hampshire June, 2009 Examining Committee: _________________________ Charles K. Barlowe, Ph.D. _________________________ William T. Wickner, M.D. _________________________ Lawrence C. Myers, Ph.D. _________________________ Jason H. Brickner, Ph.D. _________________________ Brian W. Pogue, Ph.D. Dean of Graduate Studies

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