TY - JOUR
T1 - A cholesterol-sensing mechanism unfolds
AU - Prinz, William A.
N1 - Publisher Copyright:
© 2017 by The American Society for Biochemistry and Molecular Biology, Inc.
PY - 2017/12/8
Y1 - 2017/12/8
N2 - Squalene monooxygenase (SM), which synthesizes a cholesterol precursor, is degraded when cholesterol levels in the endoplasmic reticulum (ER) membrane are high, but the signal for degradation was not known. In this issue of JBC, Brown and co-workers identify an N-terminal domain in SM that intercon-verts in a cholesterol-sensitive manner between a membrane-binding amphipathic helix and a soluble degradation-prone segment, providing the first example of a cholesterol-degron collaboration.
AB - Squalene monooxygenase (SM), which synthesizes a cholesterol precursor, is degraded when cholesterol levels in the endoplasmic reticulum (ER) membrane are high, but the signal for degradation was not known. In this issue of JBC, Brown and co-workers identify an N-terminal domain in SM that intercon-verts in a cholesterol-sensitive manner between a membrane-binding amphipathic helix and a soluble degradation-prone segment, providing the first example of a cholesterol-degron collaboration.
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U2 - 10.1074/jbc.H117.794230
DO - 10.1074/jbc.H117.794230
M3 - Article
C2 - 29222193
AN - SCOPUS:85037538745
SN - 0021-9258
VL - 292
SP - 19974
EP - 19975
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 49
ER -