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SHIP164 is a Lipid Transfer Protein that Coordinates Membrane Trafficking in the Endolysosomal System.

Record Type:	Electronic resources : Monograph/item
Title/Author:	SHIP164 is a Lipid Transfer Protein that Coordinates Membrane Trafficking in the Endolysosomal System./
Author:	Suen, Patreece H.
Description:	1 online resource (108 pages)
Notes:	Source: Dissertations Abstracts International, Volume: 85-01, Section: B.
Contained By:	Dissertations Abstracts International85-01B.
Subject:	Cellular biology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=30310563click for full text (PQDT)
ISBN:	9798379781552

SHIP164 is a Lipid Transfer Protein that Coordinates Membrane Trafficking in the Endolysosomal System.
Suen, Patreece H.

SHIP164 is a Lipid Transfer Protein that Coordinates Membrane Trafficking in the Endolysosomal System. - 1 online resource (108 pages)

Source: Dissertations Abstracts International, Volume: 85-01, Section: B.

Thesis (Ph.D.)--Yale University, 2023.

Includes bibliographical references

A defining feature of cells are membrane bilayers that separate them from their environment and, in eukaryotic cells, delineate intracellular organelles with specialized functions. In eukaryotes, the lipid composition of different organellar membranes varies both in terms of bulk and signaling lipids, lending these membranes different biochemical and biophysical characteristics. Yet most lipids are synthesized in the endoplasmic reticulum (ER), then redistributed asymmetrically from there via mechanisms that remain poorly understood. Lipid redistribution is mediated in part by lipid transport proteins that operate at membrane contact sites, where organelles are closely apposed but do not fuse, moving lipids between their membranes. Our lab and others are characterizing a new family of such proteins, called the VPS13-like proteins (or the repeating beta groove (RBG) domain family), that serve as channels for bulk lipid to flow between organelles, for example to facilitate membrane expansion. For my thesis project, my collaborators and I show that the protein SHIP164 shares structural and lipid transfer properties with this family of proteins and demonstrate that it localizes to early endocytic vesicles and contributes to their growth. Our findings raise the intriguing possibility that protein-mediated bulk lipid transfer could play a role in endosomal trafficking and maturation and support that non-vesicular protein-mediated lipid transfer is much more ubiquitous than previously appreciated.

Electronic reproduction.
Ann Arbor, Mich. :
ProQuest,
2023

Mode of access: World Wide Web

ISBN: 9798379781552Subjects--Topical Terms:

3172791
Cellular biology.
Subjects--Index Terms:

Lipid transfer proteinsIndex Terms--Genre/Form:

542853
Electronic books.

SHIP164 is a Lipid Transfer Protein that Coordinates Membrane Trafficking in the Endolysosomal System.
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520 $a A defining feature of cells are membrane bilayers that separate them from their environment and, in eukaryotic cells, delineate intracellular organelles with specialized functions. In eukaryotes, the lipid composition of different organellar membranes varies both in terms of bulk and signaling lipids, lending these membranes different biochemical and biophysical characteristics. Yet most lipids are synthesized in the endoplasmic reticulum (ER), then redistributed asymmetrically from there via mechanisms that remain poorly understood. Lipid redistribution is mediated in part by lipid transport proteins that operate at membrane contact sites, where organelles are closely apposed but do not fuse, moving lipids between their membranes. Our lab and others are characterizing a new family of such proteins, called the VPS13-like proteins (or the repeating beta groove (RBG) domain family), that serve as channels for bulk lipid to flow between organelles, for example to facilitate membrane expansion. For my thesis project, my collaborators and I show that the protein SHIP164 shares structural and lipid transfer properties with this family of proteins and demonstrate that it localizes to early endocytic vesicles and contributes to their growth. Our findings raise the intriguing possibility that protein-mediated bulk lipid transfer could play a role in endosomal trafficking and maturation and support that non-vesicular protein-mediated lipid transfer is much more ubiquitous than previously appreciated.
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