| Автор | Chang, Ta-Yuan |
| Автор | Chang, Catherine C.Y. |
| Автор | Ohgami, Nobutaka |
| Автор | Yamauchi, Yoshio |
| Дата выпуска | 2006 |
| dc.description | Abstract Mammalian cells acquire cholesterol from low-density lipoprotein (LDL) and from endogenous biosynthesis. The roles of the Niemann-Pick type C1 protein in mediating the endosomal transport of LDL-derived cholesterol and endogenously synthesized cholesterol are discussed. Excess cellular cholesterol is converted to cholesteryl esters by the enzyme acyl-coenzyme A:cholesterol acyltransferase (ACAT) 1 or is removed from a cell by cellular cholesterol efflux at the plasma membrane. A close relationship between the ACAT substrate pool and the cholesterol efflux pool is proposed. Sterol-sensing domains (SSDs) are present in several membrane proteins, including NPC1, HMG-CoA reductase, and the SREBP cleavage–activating protein. The functions of SSDs are described. ACAT1 is an endoplasmic reticulum cholesterol sensor and contains a signature motif characteristic of the membrane-bound acyltransferase family. The nonvesicular cholesterol translocation processes involve the START domain proteins and the oxysterol binding protein–related proteins (ORPs). The properties of these proteins are summarized. |
| Формат | application.pdf |
| Издатель | Annual Reviews |
| Копирайт | Annual Reviews |
| Название | Cholesterol Sensing, Trafficking, and Esterification |
| DOI | 10.1146/annurev.cellbio.22.010305.104656 |
| Print ISSN | 1081-0706 |
| Журнал | Annual Review of Cell and Developmental Biology |
| Том | 22 |
| Первая страница | 129 |
| Последняя страница | 157 |
| Аффилиация | Chang, Ta-Yuan; Department of Biochemistry, Dartmouth Medical School, Hanover, New Hampshire 03755; email: ta.yuan.chang@dartmouth.edu , catherine.c.y.chang@dartmouth.edu , yoshio.yamauchi@dartmouth.edu |
