Yeast and human P4-ATPases transport glycosphingolipids using conserved structural motifs.


Journal

The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R

Informations de publication

Date de publication:
08 02 2019
Historique:
received: 16 09 2018
revised: 29 11 2018
pubmed: 12 12 2018
medline: 27 6 2019
entrez: 12 12 2018
Statut: ppublish

Résumé

Lipid transport is an essential process with manifest importance to human health and disease. Phospholipid flippases (P4-ATPases) transport lipids across the membrane bilayer and are involved in signal transduction, cell division, and vesicular transport. Mutations in flippase genes cause or contribute to a host of diseases, such as cholestasis, neurological deficits, immunological dysfunction, and metabolic disorders. Genome-wide association studies have shown that

Identifiants

pubmed: 30530492
pii: S0021-9258(20)36829-0
doi: 10.1074/jbc.RA118.005876
pmc: PMC6369285
doi:

Substances chimiques

ATP-Binding Cassette Transporters 0
Glucosylceramides 0
Membrane Transport Proteins 0
Saccharomyces cerevisiae Proteins 0
Schizosaccharomyces pombe Proteins 0
Adenosine Triphosphatases EC 3.6.1.-
Dnf2 protein, S cerevisiae EC 3.6.1.3
ATP10A protein, human EC 7.6.2.1
Dnf1 protein, S cerevisiae EC 7.6.2.1

Banques de données

PDB
['3W5D', '1MHS', '4WIT', '3B9B', '3IXZ', '2ZXE', '3B8C', '3B8E']

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

1794-1806

Subventions

Organisme : NIGMS NIH HHS
ID : F32 GM116310
Pays : United States
Organisme : NIDDK NIH HHS
ID : P30 DK058404
Pays : United States
Organisme : NIMH NIH HHS
ID : T32 MH065215
Pays : United States
Organisme : NCI NIH HHS
ID : P30 CA068485
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM107978
Pays : United States

Informations de copyright

© 2019 Roland et al.

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Auteurs

Bartholomew P Roland (BP)

From the Department of Biological Sciences, Vanderbilt University, Nashville, Tennessee 37235 and.

Tomoki Naito (T)

the Graduate School of Pharmaceutical Science, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan.

Jordan T Best (JT)

From the Department of Biological Sciences, Vanderbilt University, Nashville, Tennessee 37235 and.

Cayetana Arnaiz-Yépez (C)

From the Department of Biological Sciences, Vanderbilt University, Nashville, Tennessee 37235 and.

Hiroyuki Takatsu (H)

the Graduate School of Pharmaceutical Science, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan.

Roger J Yu (RJ)

From the Department of Biological Sciences, Vanderbilt University, Nashville, Tennessee 37235 and.

Hye-Won Shin (HW)

the Graduate School of Pharmaceutical Science, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan.

Todd R Graham (TR)

From the Department of Biological Sciences, Vanderbilt University, Nashville, Tennessee 37235 and tr.graham@vanderbilt.edu.

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Classifications MeSH