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Peripheral myelin protein 22 preferentially partitions into ordered phase
membrane domains.
Authors Marinko JT, Kenworthy AK, Sanders CR
Submitted By Submitted Externally on 9/28/2020
Status Published
Journal Proceedings of the National Academy of Sciences of the United States of America
Year 2020
Date Published 6/1/2020
Volume : Pages 117 : 14168 - 14177
PubMed Reference 32513719
Abstract The ordered environment of cholesterol-rich membrane nanodomains is thought to
exclude many transmembrane (TM) proteins. Nevertheless, some multispan helical
transmembrane proteins have been proposed to partition into these environments.
Here, giant plasma membrane vesicles (GPMVs) were employed to quantitatively
show that the helical tetraspan peripheral myelin protein 22 (PMP22) exhibits a
pronounced preference for, promotes the formation of, and stabilizes ordered
membrane domains. Neither S-palmitoylation of PMP22 nor its putative cholesterol
binding motifs are required for this preference. In contrast,
Charcot-Marie-Tooth disease-causing mutations that disrupt the stability of
PMP22 tertiary structure reduce or eliminate this preference in favor of the
disordered phase. These studies demonstrate that the ordered phase preference of
PMP22 derives from global structural features associated with the folded form of
this protein, providing a glimpse at the structural factors that promote raft
partitioning for multispan helical membrane proteins.


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