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Fusion proteins and select lipids cooperate as membrane receptors for the soluble snare Vam7p / by Vidya Karunakaran.

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Author	Karunakaran, Vidya.
Title	Fusion proteins and select lipids cooperate as membrane receptors for the soluble snare Vam7p / by Vidya Karunakaran.
Date	2014
Abstract	Yeast vacuole fusion involves three transmembrane SNAREs and a unique soluble SNARE, Vam7p. This SNARE cycles between vacuolar membrane-bound and cytosolic state. In its membrane-bound state, it is able to participate in vacuolar fusion by complexing with the other SNAREs. Vam7p is drawn from a cytosolic pool to the vacuolar membrane. As a means to this end, Vam7p has evolved a lipid-binding PX domain. Vam7p is recruited to the membrane by the affinities of its PX domain for the lipid PI(3)P on the vacuolar membrane and for the tethering complex HOPS. The Vam7p SNARE domain also has an affinity for the SNARE domains of the other vacuolar SNAREs. The complexity of the in vivo vacuolar environment complicates studies of binding interactions. The reconstitution of in vitro vacuole fusion with purified SNAREs, Rab, and HOPS in proteoliposomes bearing vacuolar mimic lipid compositions offered an opportunity to establish the minimal affinities required for Vam7p recruitment to the membrane. In vitro sedimentation-based binding assays, used in conjunction with F?rster resonance energy transfer (FRET) assays capable of quantifying lipid mixing, fusion and lysis, have allowed us to establish a set of receptors for Vam7p-membrane binding. We also establish the functional requirement for a non-specific electrostatic interaction of Vam7p with anionic lipids that is mediated through the PX domain. We conclude that the product of these several moderate affinities for HOPS, PI(3)P, anionic lipids and SNAREs contribute to a high affinity biological interaction
Description	ix, 139 leaves : ill. (some col.)
Format	application/pdf
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.1233

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