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A Bipartite Sorting Signal Ensures S...

Chuang, Ya-Shan.

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A Bipartite Sorting Signal Ensures Specificity of Retromer Complex in Membrane Protein Recycling.

Record Type:	Electronic resources : Monograph/item
Title/Author:	A Bipartite Sorting Signal Ensures Specificity of Retromer Complex in Membrane Protein Recycling./
Author:	Chuang, Ya-Shan.
Published:	Ann Arbor : ProQuest Dissertations & Theses, : 2019,
Description:	245 p.
Notes:	Source: Dissertations Abstracts International, Volume: 81-04, Section: B.
Contained By:	Dissertations Abstracts International81-04B.
Subject:	Cellular biology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=22615817
ISBN:	9781088378120

A Bipartite Sorting Signal Ensures Specificity of Retromer Complex in Membrane Protein Recycling.
Chuang, Ya-Shan.

A Bipartite Sorting Signal Ensures Specificity of Retromer Complex in Membrane Protein Recycling. - Ann Arbor : ProQuest Dissertations & Theses, 2019 - 245 p.

Source: Dissertations Abstracts International, Volume: 81-04, Section: B.

Thesis (Ph.D.)--Cornell University, 2019.

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

In the endosomal network, membrane proteins are either sorted into intraluminal vesicles for the lysosomal degradative pathway or exported from the endosome to the trans-Golgi network (TGN) via retrograde transport. Retromer is an evolutionarily conserved protein complex, which sorts functionally diverse membrane proteins into recycling tubules/vesicles from the endosome. Many of the identified cargos possess a recycling signal sequence defined as OX[L/M/V], where O is a bulky aromatic residue and X could be any residue. However, this sequence is present in almost all proteins encoded in the genome. Also, several identified recycling sequences do not follow this rule. How retromer precisely selects its cargos remains unclear.Here, we reveal that an additional motif is also required for cargo retrieval. The two distinct motifs form a bipartite recycling signal recognized by the retromer subunits, Vps26 and Vps35. Strikingly, Vps26 utilizes different binding sites depending on the cargo, allowing retromer to recycle different membrane proteins. Thus, the complicated interaction between the retromer complex and cargoes increases the diversity and specificity in the recognition of cargo recycling.

ISBN: 9781088378120Subjects--Topical Terms:

3172791
Cellular biology.
Subjects--Index Terms:

CPY

A Bipartite Sorting Signal Ensures Specificity of Retromer Complex in Membrane Protein Recycling.
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020 $a 9781088378120
035 $a (MiAaPQ)AAI22615817
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100 1 $a Chuang, Ya-Shan. $3 3550156
245 1 0 $a A Bipartite Sorting Signal Ensures Specificity of Retromer Complex in Membrane Protein Recycling.
260 1 $a Ann Arbor : $b ProQuest Dissertations & Theses, $c 2019
300 $a 245 p.
500 $a Source: Dissertations Abstracts International, Volume: 81-04, Section: B.
500 $a Advisor: Emr, Scott.
502 $a Thesis (Ph.D.)--Cornell University, 2019.
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 In the endosomal network, membrane proteins are either sorted into intraluminal vesicles for the lysosomal degradative pathway or exported from the endosome to the trans-Golgi network (TGN) via retrograde transport. Retromer is an evolutionarily conserved protein complex, which sorts functionally diverse membrane proteins into recycling tubules/vesicles from the endosome. Many of the identified cargos possess a recycling signal sequence defined as OX[L/M/V], where O is a bulky aromatic residue and X could be any residue. However, this sequence is present in almost all proteins encoded in the genome. Also, several identified recycling sequences do not follow this rule. How retromer precisely selects its cargos remains unclear.Here, we reveal that an additional motif is also required for cargo retrieval. The two distinct motifs form a bipartite recycling signal recognized by the retromer subunits, Vps26 and Vps35. Strikingly, Vps26 utilizes different binding sites depending on the cargo, allowing retromer to recycle different membrane proteins. Thus, the complicated interaction between the retromer complex and cargoes increases the diversity and specificity in the recognition of cargo recycling.
590 $a School code: 0058.
650 4 $a Cellular biology. $3 3172791
650 4 $a Molecular biology. $3 517296
653 $a CPY
653 $a Ear1
653 $a Recycling
653 $a Retromer
653 $a Rsp5
653 $a Vps10
690 $a 0379
690 $a 0307
710 2 $a Cornell University. $b Biochemistry, Molecular and Cell Biology. $3 3437957
773 0 $t Dissertations Abstracts International $g 81-04B.
790 $a 0058
791 $a Ph.D.
792 $a 2019
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=22615817