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Functional analysis of Aut7 in vacuo...

Huang, Wei-Pang.

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Functional analysis of Aut7 in vacuolar delivery of aminopeptidase I in Saccharomyces cerevisiae.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Functional analysis of Aut7 in vacuolar delivery of aminopeptidase I in Saccharomyces cerevisiae./
Author:	Huang, Wei-Pang.
Published:	Ann Arbor : ProQuest Dissertations & Theses, : 2002,
Description:	113 p.
Notes:	Source: Dissertations Abstracts International, Volume: 64-07, Section: B.
Contained By:	Dissertations Abstracts International64-07B.
Subject:	Cellular biology. -
Online resource:	https://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3065258
ISBN:	9780493841724

Functional analysis of Aut7 in vacuolar delivery of aminopeptidase I in Saccharomyces cerevisiae.
Huang, Wei-Pang.

Functional analysis of Aut7 in vacuolar delivery of aminopeptidase I in Saccharomyces cerevisiae. - Ann Arbor : ProQuest Dissertations & Theses, 2002 - 113 p.

Source: Dissertations Abstracts International, Volume: 64-07, Section: B.

Thesis (Ph.D.)--University of California, Davis, 2002.

This item must not be sold to any third party vendors.

The vacuole of Saccharomyces cerevisiae participates in multiple cellular activities important for yeast physiology. One of its major functions is to turnover long-lived proteins and subcellular organelles. The mechanisms for resident enzyme and substrate delivery to the vacuole are important model systems for protein targeting studies in cell biology. To our surprise, the vacuolar resident hydrolase aminopeptidase 1 (Ape1) does not follow conventional routes for transport as do the majority of vacuolar enzymes. Precursors of Ape1 (prApe1) are delivered directly from cytoplasm to the vacuole by the cytoplasm-to-vacuole targeting (Cvt) pathway. The Cvt pathway shares partially overlapped machinery with the degradative vacuolar transport mechanism autophagy. Autophagy is generally operated in a non-specific aspect, but prApe1 import is mediated by autophagy pathway under starvation conditions. In addition, specific peroxisome degradation in Saccharomyces cerevisiae also requires most autophagy components, indicating that the same set of machinery can be directed for different vacuolar transport pathways. Between the overlapped Apg and Cvt proteins, we have characterized Aut7 as the first starvation inducible component. Aut7 function is required for transport vesicle formation for both the Cvt pathway and autophagy. After finishing the vacuolar transport activity, Aut7 is degraded inside of the vacuole together with transport cargo. These properties indicate that Aut7 is a structural component of the sequestering membrane. We have found that membrane recruitment of Aut7 required two novel autophagy conjugation systems. Most of these components required for Aut7 recruitment locate to a perivacuolar structure. Aut7 dose not interact intensely with proteins constituting the two novel conjugation systems but co-isolates prApe1 and its receptor/adaptor Cvt19. We have characterized this interaction as the sorting mechanism for prApe1 import. This work broadens our perspective on autophagy mechanism and provides a basis for the study of autophagy-related human diseases.

ISBN: 9780493841724Subjects--Topical Terms:

3172791
Cellular biology.
Subjects--Index Terms:

Aminopeptidase

Functional analysis of Aut7 in vacuolar delivery of aminopeptidase I in Saccharomyces cerevisiae.
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245 1 0 $a Functional analysis of Aut7 in vacuolar delivery of aminopeptidase I in Saccharomyces cerevisiae.
260 1 $a Ann Arbor : $b ProQuest Dissertations & Theses, $c 2002
300 $a 113 p.
500 $a Source: Dissertations Abstracts International, Volume: 64-07, Section: B.
500 $a Publisher info.: Dissertation/Thesis.
500 $a Advisor: Klisnsky, Daniel.
502 $a Thesis (Ph.D.)--University of California, Davis, 2002.
506 $a This item must not be sold to any third party vendors.
506 $a This item must not be added to any third party search indexes.
520 $a The vacuole of Saccharomyces cerevisiae participates in multiple cellular activities important for yeast physiology. One of its major functions is to turnover long-lived proteins and subcellular organelles. The mechanisms for resident enzyme and substrate delivery to the vacuole are important model systems for protein targeting studies in cell biology. To our surprise, the vacuolar resident hydrolase aminopeptidase 1 (Ape1) does not follow conventional routes for transport as do the majority of vacuolar enzymes. Precursors of Ape1 (prApe1) are delivered directly from cytoplasm to the vacuole by the cytoplasm-to-vacuole targeting (Cvt) pathway. The Cvt pathway shares partially overlapped machinery with the degradative vacuolar transport mechanism autophagy. Autophagy is generally operated in a non-specific aspect, but prApe1 import is mediated by autophagy pathway under starvation conditions. In addition, specific peroxisome degradation in Saccharomyces cerevisiae also requires most autophagy components, indicating that the same set of machinery can be directed for different vacuolar transport pathways. Between the overlapped Apg and Cvt proteins, we have characterized Aut7 as the first starvation inducible component. Aut7 function is required for transport vesicle formation for both the Cvt pathway and autophagy. After finishing the vacuolar transport activity, Aut7 is degraded inside of the vacuole together with transport cargo. These properties indicate that Aut7 is a structural component of the sequestering membrane. We have found that membrane recruitment of Aut7 required two novel autophagy conjugation systems. Most of these components required for Aut7 recruitment locate to a perivacuolar structure. Aut7 dose not interact intensely with proteins constituting the two novel conjugation systems but co-isolates prApe1 and its receptor/adaptor Cvt19. We have characterized this interaction as the sorting mechanism for prApe1 import. This work broadens our perspective on autophagy mechanism and provides a basis for the study of autophagy-related human diseases.
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791 $a Ph.D.
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793 $a English
856 4 0 $u https://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3065258