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Structure based biophysical characterization of the PROPPIN Atg18 shows Atg18 oligomerization upon membrane binding

Overview of attention for article published in Scientific Reports, October 2017
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Title
Structure based biophysical characterization of the PROPPIN Atg18 shows Atg18 oligomerization upon membrane binding
Published in
Scientific Reports, October 2017
DOI 10.1038/s41598-017-14337-5
Pubmed ID
Authors

Andreea Scacioc, Carla Schmidt, Tommy Hofmann, Henning Urlaub, Karin Kühnel, Ángel Pérez-Lara

Abstract

PROPPINs (β-propellers that bind polyphosphoinositides) are PtdIns3P and PtdIns(3,5)P2 binding autophagy related proteins. They contain two phosphatidylinositolphosphate (PIP) binding sites and a conserved FRRG motif is essential for PIP binding. Here we present the 2.0 Å resolution crystal structure of the PROPPIN Atg18 from Pichia angusta. We designed cysteine mutants for labelling with the fluorescence dyes to probe the distances of the mutants to the membrane. These measurements support a model for PROPPIN-membrane binding, where the PROPPIN sits in a perpendicular or slightly tilted orientation on the membrane. Stopped-flow measurements suggest that initial PROPPIN-membrane binding is driven by non-specific PIP interactions. The FRRG motif then retains the protein in the membrane by binding two PIP molecules as evident by a lower dissociation rate for Atg18 in comparison with its PIP binding deficient FTTG mutant. We demonstrate that the amine-specific cross-linker Bis(sulfosuccinimidyl)suberate (BS3), which is used for protein-protein cross-linking can also be applied for cross-linking proteins and phosphatidylethanolamine (PE). Cross-linking experiments with liposome bound Atg18 yielded several PE cross-linked peptides. We also observed intermolecular cross-linked peptides, which indicated Atg18 oligomerization. FRET-based stopped-flow measurements revealed that Atg18 rapidly oligomerizes upon membrane binding while it is mainly monomeric in solution.

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Mendeley readers

The data shown below were compiled from readership statistics for 16 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 16 100%

Demographic breakdown

Readers by professional status Count As %
Researcher 5 31%
Student > Master 4 25%
Student > Ph. D. Student 3 19%
Unspecified 3 19%
Professor > Associate Professor 1 6%
Other 0 0%
Readers by discipline Count As %
Agricultural and Biological Sciences 8 50%
Biochemistry, Genetics and Molecular Biology 3 19%
Unspecified 3 19%
Computer Science 1 6%
Neuroscience 1 6%
Other 0 0%

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 03 November 2017.
All research outputs
#9,669,646
of 12,091,568 outputs
Outputs from Scientific Reports
#38,351
of 53,802 outputs
Outputs of similar age
#206,534
of 284,599 outputs
Outputs of similar age from Scientific Reports
#4,224
of 6,561 outputs
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