[HTML][HTML] Overexpression of membrane domain of SCAP prevents sterols from inhibiting SCAP· SREBP exit from endoplasmic reticulum
T Yang, JL Goldstein, MS Brown - Journal of Biological Chemistry, 2000 - ASBMB
SCAP (SREBP cleavage-activating protein) forms a complex with sterol regulatory element-
binding proteins (SREBPs) and escorts them from the endoplasmic reticulum (ER) to the
Golgi complex where proteases release transcriptionally active segments of SREBPs, which
enter the nucleus to activate lipid synthesis. The NH 2-terminal segment of SCAP contains
eight transmembrane helices, five of which (TM2–6) comprise the sterol-sensing domain.
This domain responds to sterols by causing the SCAP· SREBP complex to be retained in the …
binding proteins (SREBPs) and escorts them from the endoplasmic reticulum (ER) to the
Golgi complex where proteases release transcriptionally active segments of SREBPs, which
enter the nucleus to activate lipid synthesis. The NH 2-terminal segment of SCAP contains
eight transmembrane helices, five of which (TM2–6) comprise the sterol-sensing domain.
This domain responds to sterols by causing the SCAP· SREBP complex to be retained in the …