Membrane Binding of Recoverin: From Mechanistic Understanding
to Biological Functionality
Version 3 2017-08-23, 04:18
Version 2 2017-07-24, 13:20
Version 1 2017-07-24, 12:33
Posted on 2017-08-23 - 04:18
Recoverin is a neuronal
calcium sensor involved in vision adaptation
that reversibly associates with cellular membranes via its calcium-activated
myristoyl switch. While experimental evidence shows that the myristoyl
group significantly enhances membrane affinity of this protein, molecular
details of the binding process are still under debate. Here, we present
results of extensive molecular dynamics simulations of recoverin in
the proximity of a phospholipid bilayer. We capture multiple events
of spontaneous membrane insertion of the myristoyl moiety and confirm
its critical role in the membrane binding. Moreover, we observe that
the binding strongly depends on the conformation of the N-terminal
domain. We propose that a suitable conformation of the N-terminal
domain can be stabilized by the disordered C-terminal segment or by
binding of the target enzyme, i.e., rhodopsin kinase. Finally, we
find that the presence of negatively charged lipids in the bilayer
stabilizes a physiologically functional orientation of the membrane-bound
recoverin.
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Timr, Štěpán; Pleskot, Roman; Kadlec, Jan; Kohagen, Miriam; Magarkar, Aniket; Jungwirth, Pavel (2017). Membrane Binding of Recoverin: From Mechanistic Understanding
to Biological Functionality. ACS Publications. Collection. https://doi.org/10.1021/acscentsci.7b00210
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AUTHORS (6)
ST
Štěpán Timr
RP
Roman Pleskot
JK
Jan Kadlec
MK
Miriam Kohagen
AM
Aniket Magarkar
PJ
Pavel Jungwirth