Flexible and Extended Linker Domains Support Efficient Targeting of Heh2 to the Inner Nuclear Membrane.
Saccharomyces cerevisiae
intrinsically disordered domain
membrane protein
nuclear pore complex
nuclear transport
Journal
Structure (London, England : 1993)
ISSN: 1878-4186
Titre abrégé: Structure
Pays: United States
ID NLM: 101087697
Informations de publication
Date de publication:
04 02 2020
04 02 2020
Historique:
received:
08
04
2019
revised:
09
08
2019
accepted:
08
11
2019
pubmed:
7
12
2019
medline:
30
4
2021
entrez:
7
12
2019
Statut:
ppublish
Résumé
The nuclear pore complex (NPC) is embedded in the nuclear envelope and forms the main gateway to the nuclear interior including the inner nuclear membrane (INM). Two INM proteins in yeast are selectively imported. Their sorting signals consist of a nuclear localization signal, separated from the transmembrane domain by a long intrinsically disordered (ID) linker. We used computational models to predict the dynamic conformations of ID linkers and analyzed the INM targeting efficiency of proteins with linker regions with altered Stokes radii and decreased flexibilities. We find that flexibility, Stokes radius, and the frequency at which the linkers are at an extended end-to-end distance larger than 25 nm are good predictors for the targeting of the proteins. The data are consistent with a transport mechanism in which INM targeting of Heh2 is dependent on an ID linker that facilitates the crossing of the approximately 25-nm thick NPC scaffold.
Identifiants
pubmed: 31806352
pii: S0969-2126(19)30387-9
doi: 10.1016/j.str.2019.11.003
pii:
doi:
Substances chimiques
Heh2 protein, S cerevisiae
0
Membrane Proteins
0
Nuclear Proteins
0
Protein Sorting Signals
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
185-195.e5Informations de copyright
Copyright © 2019 Elsevier Ltd. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Interests The authors declare no competing interests.