Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0201826
Title: ATP competes with PIP 2 for binding to gelsolin
Authors: Szatmári D.
Xue B. 
Kannan B.
Burtnick L.D.
Bugyi B.
Nyitrai M.
Robinson R.C. 
Keywords: adenosine triphosphate
calcium
gelsolin
phosphatidylinositol 4,5 bisphosphate
phospholipid
sodium chloride
actin
adenosine triphosphate
cation
gelsolin
magnesium
phosphatidylinositol 4,5 bisphosphate
protein binding
actin filament
anisotropy
Article
cell membrane
controlled study
cytoplasm
enzyme activity
enzyme regulation
fluorescence
human
human cell
in vitro study
protein binding
protein function
protein protein interaction
protein secretion
steady state
animal
binding competition
Escherichia coli
kinetics
Leporidae
metabolism
polymerization
Actins
Adenosine Triphosphate
Animals
Binding, Competitive
Calcium
Cations
Cell Membrane
Escherichia coli
Gelsolin
Humans
Kinetics
Magnesium
Phosphatidylinositol 4,5-Diphosphate
Polymerization
Protein Binding
Rabbits
Issue Date: 2018
Citation: Szatmári D., Xue B., Kannan B., Burtnick L.D., Bugyi B., Nyitrai M., Robinson R.C. (2018). ATP competes with PIP 2 for binding to gelsolin. PLoS ONE 13 (8) : e0201826. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0201826
Rights: Attribution 4.0 International
Abstract: Gelsolin is a severing and capping protein that targets filamentous actin and regulates filament lengths near plasma membranes, contributing to cell movement and plasma membrane morphology. Gelsolin binds to the plasma membrane via phosphatidylinositol 4,5-bisphosphate (PIP 2 ) in a state that cannot cap F-actin, and gelsolin-capped actin filaments are uncapped by PIP 2 leading to filament elongation. The process by which gelsolin is removed from PIP 2 at the plasma membrane is currently unknown. Gelsolin also binds ATP with unknown function. Here we characterize the role of ATP on PIP 2 -gelsolin complex dynamics. Fluorophore-labeled PIP 2 and ATP were used to study their interactions with gelsolin using steady-state fluorescence anisotropy, and Alexa488-labeled gelsolin was utilized to reconstitute the regulation of gelsolin binding to PIP 2 -containing phospholipid vesicles by ATP. Under physiological salt conditions ATP competes with PIP 2 for binding to gelsolin, while calcium causes the release of ATP from gelsolin. These data suggest a cycle for gelsolin activity. Firstly, calcium activates ATP-bound gelsolin allowing it to sever and cap F-actin. Secondly, PIP 2 -binding removes the gelsolin cap from F-actin at low calcium levels, leading to filament elongation. Finally, ATP competes with PIP 2 to release the calcium-free ATP-bound gelsolin, allowing it to undergo a further round of severing. © 2018 Szatmári et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Source Title: PLoS ONE
URI: https://scholarbank.nus.edu.sg/handle/10635/161218
ISSN: 19326203
DOI: 10.1371/journal.pone.0201826
Rights: Attribution 4.0 International
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This item is licensed under a Creative Commons License Creative Commons