Membrane Lipid Requirements of the Lysine Transporter Lyp1 from Saccharomyces cerevisiae.

Amino Acid Transport Systems, Basic / genetics Cell Membrane / genetics Kinetics Lysine / metabolism Membrane Lipids / genetics Membrane Transport Proteins / genetics Saccharomyces cerevisiae / genetics Saccharomyces cerevisiae Proteins / genetics
APC superfamily Saccharomyces cerevisiae amino acids membrane transport yeast plasma membrane

Journal

Journal of molecular biology
ISSN: 1089-8638
Titre abrégé: J Mol Biol
Pays: Netherlands
ID NLM: 2985088R

Informations de publication

Date de publication:
26 06 2020
Historique:
received: 06 04 2020
revised: 28 04 2020
accepted: 30 04 2020
pubmed: 16 5 2020
medline: 29 12 2020
entrez: 16 5 2020
Statut: ppublish

Résumé

Membrane lipids act as solvents and functional cofactors for integral membrane proteins. The yeast plasma membrane is unusual in that it may have a high lipid order, which coincides with low passive permeability for small molecules and a slow lateral diffusion of proteins. Yet, membrane proteins whose functions require altered conformation must have flexibility within membranes. We have determined the molecular composition of yeast plasma membrane lipids located within a defined diameter of model proteins, including the APC-superfamily lysine transporter Lyp1. We now use the composition of lipids that naturally surround Lyp1 to guide testing of lipids that support the normal functioning of the transporter, when reconstituted in vesicles of defined lipid composition. We find that phosphatidylserine and ergosterol are essential for Lyp1 function, and the transport activity displays a sigmoidal relationship with the concentration of these lipids. Non-bilayer lipids stimulate transport activity, but different types are interchangeable. Remarkably, Lyp1 requires a relatively high fraction of lipids with one or more unsaturated acyl chains. The transport data and predictions of the periprotein lipidome of Lyp1 support a new model in which a narrow band of lipids immediately surrounding the transmembrane stalk of a model protein allows conformational changes in the protein.

Identifiants

DOI: 10.1016/j.jmb.2020.04.029 PMID: 32413406 PMC: PMC8005870
pubmed: 32413406
pii: S0022-2836(20)30332-6
doi: 10.1016/j.jmb.2020.04.029
pmc: PMC8005870
mid: NIHMS1681749
pii:
doi:

Substances chimiques

Amino Acid Transport Systems, Basic 0
LYP1 protein, S cerevisiae 0
Membrane Lipids 0
Membrane Transport Proteins 0
Saccharomyces cerevisiae Proteins 0
Lysine K3Z4F929H6

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

4023-4031

Subventions

Organisme : NIAMS NIH HHS
ID : R01 AR048632
Pays : United States

Informations de copyright

Copyright © 2020 The Authors. Published by Elsevier Ltd.. All rights reserved.

Déclaration de conflit d'intérêts

Conflict of Interest The authors declare no conflict of interest

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Auteurs

Joury S van 't Klooster (JS)

Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747, AG, Groningen, the Netherlands.

Tan-Yun Cheng (TY)

Division of Rheumatology, Inflammation and Immunity, Brigham and Women's Hospital, Harvard Medical School, 60 Fenwood Road, Boston, MA 02115, USA.

Hendrik R Sikkema (HR)

Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747, AG, Groningen, the Netherlands.

Aike Jeucken (A)

Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747, AG, Groningen, the Netherlands.

D Branch Moody (DB)

Division of Rheumatology, Inflammation and Immunity, Brigham and Women's Hospital, Harvard Medical School, 60 Fenwood Road, Boston, MA 02115, USA; Department of Medicine, Harvard Medical School, Boston, MA 02115, USA.

Bert Poolman (B)

Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747, AG, Groningen, the Netherlands. Electronic address: b.poolman@rug.nl.

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Classifications MeSH

questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines membranaires › Protéines de transport membranaire › Systèmes de transport d'acides aminés › Systèmes de transport d'acides aminés basiques › Membrane Lipid Requirements of the Lysine...
questionsmedicales.fr › Cellules › Structures cellulaires › Membrane cellulaire › Membrane Lipid Requirements of the Lysine...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Cinétique › Membrane Lipid Requirements of the Lysine...
questionsmedicales.fr › Acides aminés, peptides et protéines › Acides aminés › Acides aminés essentiels › Lysine › Membrane Lipid Requirements of the Lysine...
questionsmedicales.fr › Lipides › Lipides membranaires › Membrane Lipid Requirements of the Lysine...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines membranaires › Protéines de transport membranaire › Membrane Lipid Requirements of the Lysine...
questionsmedicales.fr › Eucaryotes › Champignons › Levures › Saccharomyces › Saccharomyces cerevisiae › Membrane Lipid Requirements of the Lysine...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines fongiques › Protéines de Saccharomyces cerevisiae › Membrane Lipid Requirements of the Lysine...