Biophysical Parameters of the Sec14 Phospholipid Exchange Cycle.


Journal

Biophysical journal
ISSN: 1542-0086
Titre abrégé: Biophys J
Pays: United States
ID NLM: 0370626

Informations de publication

Date de publication:
08 01 2019
Historique:
received: 21 09 2018
revised: 24 10 2018
accepted: 28 11 2018
pubmed: 26 12 2018
medline: 3 1 2020
entrez: 25 12 2018
Statut: ppublish

Résumé

Sec14, the major yeast phosphatidylcholine (PC)/phosphatidylinositol (PI) transfer protein (PITP), coordinates PC and PI metabolism to facilitate an appropriate and essential lipid signaling environment for membrane trafficking from trans-Golgi membranes. The Sec14 PI/PC exchange cycle is essential for its essential biological activity, but fundamental aspects of how this PITP executes its lipid transfer cycle remain unknown. To address some of these outstanding issues, we applied time-resolved small-angle neutron scattering for the determination of protein-mediated intervesicular movement of deuterated and hydrogenated phospholipids in vitro. Quantitative analysis by small-angle neutron scattering revealed that Sec14 PI- and PC-exchange activities were sensitive to both the lipid composition and curvature of membranes. Moreover, we report that these two parameters regulate lipid exchange activity via distinct mechanisms. Increased membrane curvature promoted both membrane binding and lipid exchange properties of Sec14, indicating that this PITP preferentially acts on the membrane site with a convexly curved face. This biophysical property likely constitutes part of a mechanism by which spatial specificity of Sec14 function is determined in cells. Finally, wild-type Sec14, but not a mixture of Sec14 proteins specifically deficient in either PC- or PI-binding activity, was able to effect a net transfer of PI or PC down opposing concentration gradients in vitro.

Identifiants

pubmed: 30580923
pii: S0006-3495(18)34453-9
doi: 10.1016/j.bpj.2018.11.3131
pmc: PMC6342728
pii:
doi:

Substances chimiques

Phosphatidylcholines 0
Phosphatidylinositols 0
Phospholipid Transfer Proteins 0
SEC14 protein, S cerevisiae 0
Saccharomyces cerevisiae Proteins 0
Unilamellar Liposomes 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

92-103

Subventions

Organisme : NIGMS NIH HHS
ID : R01 GM044530
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM131804
Pays : United States

Informations de copyright

Copyright © 2018 Biophysical Society. All rights reserved.

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Auteurs

Taichi Sugiura (T)

Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama, Toyama, Japan.

Chisato Takahashi (C)

Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto, Japan.

Yusuke Chuma (Y)

Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto, Japan.

Masakazu Fukuda (M)

Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto, Japan.

Makiko Yamada (M)

Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto, Japan.

Ukyo Yoshida (U)

Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama, Toyama, Japan.

Hiroyuki Nakao (H)

Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama, Toyama, Japan.

Keisuke Ikeda (K)

Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama, Toyama, Japan.

Danish Khan (D)

Departments of Biochemistry and Biophysics, Texas A&M University, College Station, Texas.

Aaron H Nile (AH)

Department of Molecular & Cellular Medicine, Texas A&M Health Sciences Center, College Station, Texas.

Vytas A Bankaitis (VA)

Departments of Biochemistry and Biophysics, Texas A&M University, College Station, Texas; Department of Molecular & Cellular Medicine, Texas A&M Health Sciences Center, College Station, Texas.

Minoru Nakano (M)

Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama, Toyama, Japan. Electronic address: mnakano@pha.u-toyama.ac.jp.

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Classifications MeSH