The N-terminal Domain of NPC1L1 Protein Binds Cholesterol and Plays Essential Roles in Cholesterol Uptake
نویسندگان
چکیده
منابع مشابه
The N-terminal Domain of Npc1l1 Binds Cholesterol and Plays Essential Roles in Cholesterol Uptake
ROLES IN CHOLESTEROL UPTAKE Jin-Hui Zhang , Liang Ge , Wei Qi , Liqing Zhang, Hong-Hua Miao, Bo-Liang Li, Maojun Yang and Bao-Liang Song 2 From The State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, 320 Yue-Yang Road, Shanghai 200031, China and MOE Key Laboratory of Bioinformatics, Scho...
متن کاملEzetimibe-sensitive cholesterol uptake by NPC1L1 protein does not require endocytosis
Human NPC1L1 protein mediates cholesterol absorption in the intestine and liver and is the target of the drug ezetimibe, which is used to treat hypercholesterolemia. Previous studies concluded that NPC1L1-GFP protein trafficking is regulated by cholesterol binding and that ezetimibe blocks NPC1L1-GFP function by inhibiting its endocytosis. We used cell surface biotinylation to monitor NPC1L1-GF...
متن کاملThe Plasmodium falciparum rhoptry protein RhopH3 plays essential roles in host cell invasion and nutrient uptake
Merozoites of the protozoan parasite responsible for the most virulent form of malaria, Plasmodium falciparum, invade erythrocytes. Invasion involves discharge of rhoptries, specialized secretory organelles. Once intracellular, parasites induce increased nutrient uptake by generating new permeability pathways (NPP) including a Plasmodium surface anion channel (PSAC). RhopH1/Clag3, one member of...
متن کاملRetinoblastoma protein plays multiple essential roles in the terminal differentiation of Sertoli cells.
Retinoblastoma protein (RB) plays crucial roles in cell cycle control and cellular differentiation. Specifically, RB impairs the G(1) to S phase transition by acting as a repressor of the E2F family of transcriptional activators while also contributing towards terminal differentiation by modulating the activity of tissue-specific transcription factors. To examine the role of RB in Sertoli cells...
متن کاملThe amyloid precursor protein has a flexible transmembrane domain and binds cholesterol.
C99 is the transmembrane carboxyl-terminal domain of the amyloid precursor protein that is cleaved by γ-secretase to release the amyloid-β polypeptides, which are associated with Alzheimer's disease. Nuclear magnetic resonance and electron paramagnetic resonance spectroscopy show that the extracellular amino terminus of C99 includes a surface-embedded "N-helix" followed by a short "N-loop" conn...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2011
ISSN: 0021-9258
DOI: 10.1074/jbc.m111.244475