Exchange of water for sterol underlies sterol egress from a StARkin domain.


Journal

eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614

Informations de publication

Date de publication:
04 12 2019
Historique:
received: 11 11 2019
accepted: 29 11 2019
pubmed: 5 12 2019
medline: 27 5 2020
entrez: 5 12 2019
Statut: epublish

Résumé

Previously we identified Lam/GramD1 proteins, a family of endoplasmic reticulum membrane proteins with sterol-binding StARkin domains that are implicated in intracellular sterol homeostasis. Here, we show how these proteins exchange sterol molecules with membranes. An aperture at one end of the StARkin domain enables sterol to enter/exit the binding pocket. Strikingly, the wall of the pocket is longitudinally fractured, exposing bound sterol to solvent. Large-scale atomistic molecular dynamics simulations reveal that sterol egress involves widening of the fracture, penetration of water into the cavity, and consequent destabilization of the bound sterol. The simulations identify polar residues along the fracture that are important for sterol release. Their replacement with alanine affects the ability of the StARkin domain to bind sterol, catalyze inter-vesicular sterol exchange and alleviate the nystatin-sensitivity of

Identifiants

pubmed: 31799930
doi: 10.7554/eLife.53444
pii: 53444
pmc: PMC6940019
doi:
pii:

Substances chimiques

Antiporters 0
DNA-Binding Proteins 0
LRP1 protein, S cerevisiae 0
LTC1 protein, S cerevisiae 0
Membrane Proteins 0
Nuclear Proteins 0
RNA-Binding Proteins 0
Saccharomyces cerevisiae Proteins 0
Sterols 0
Water 059QF0KO0R
Exosome Multienzyme Ribonuclease Complex EC 3.1.-

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

Subventions

Organisme : NIA NIH HHS
ID : R37 AG019391
Pays : United States
Organisme : NIH HHS
ID : R37AG019391
Pays : United States

Informations de copyright

© 2019, Khelashvili et al.

Déclaration de conflit d'intérêts

GK, NC, KP, DE, AM No competing interests declared

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Auteurs

George Khelashvili (G)

Department of Physiology and Biophysics, Weill Cornell Medical College, New York, United States.
Institute for Computational Biomedicine, Weill Cornell Medical College, New York, United States.

Neha Chauhan (N)

Department of Biochemistry, Weill Cornell Medical College, New York, United States.

Kalpana Pandey (K)

Department of Biochemistry, Weill Cornell Medical College, New York, United States.

David Eliezer (D)

Department of Biochemistry, Weill Cornell Medical College, New York, United States.

Anant K Menon (AK)

Department of Biochemistry, Weill Cornell Medical College, New York, United States.

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Classifications MeSH