Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26551077
&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests
in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215
Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\26551077
.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117 Nat+Struct+Mol+Biol
2015 ; 22
(12
): 991-8
Nephropedia Template TP
gab.com Text
Twit Text FOAVip
Twit Text #
English Wikipedia
The role of lipids in mechanosensation
#MMPMID26551077
Pliotas C
; Dahl AC
; Rasmussen T
; Mahendran KR
; Smith TK
; Marius P
; Gault J
; Banda T
; Rasmussen A
; Miller S
; Robinson CV
; Bayley H
; Sansom MS
; Booth IR
; Naismith JH
Nat Struct Mol Biol
2015[Dec]; 22
(12
): 991-8
PMID26551077
show ga
The ability of proteins to sense membrane tension is pervasive in biology. A
higher-resolution structure of the Escherichia coli small-conductance
mechanosensitive channel MscS identifies alkyl chains inside pockets formed by
the transmembrane helices (TMs). Purified MscS contains E. coli lipids, and
fluorescence quenching demonstrates that phospholipid acyl chains exchange
between bilayer and TM pockets. Molecular dynamics and biophysical analyses show
that the volume of the pockets and thus the number of lipid acyl chains within
them decreases upon channel opening. Phospholipids with one acyl chain per head
group (lysolipids) displace normal phospholipids (with two acyl chains) from MscS
pockets and trigger channel opening. We propose that the extent of acyl-chain
interdigitation in these pockets determines the conformation of MscS. When
interdigitation is perturbed by increased membrane tension or by lysolipids, the
closed state becomes unstable, and the channel gates.
free
free
free
