The low-density lipoprotein receptor (LDLR) is a critical determinant of plasma cholesterol levels that internalizes lipoprotein cargo via clathrin-mediated endocytosis. Here, we show that the E3 ubiquitin ligase IDOL stimulates a previously unrecognized, clathrin-independent pathway for LDLR internalization.
IDOL Stimulates Clathrin-Independent Endocytosis and Multivesicular Body-Mediated Lysosomal Degradation of the Low-Density Lipoprotein Receptor / E. Scotti;M. Calamai;C. N. Goulbourne;L. Zhang;C. Hong;R. R. Lin;J. Choi;P. F. Pilch;L. G. Fong;P. Zou;A. Y. Ting;F. S. Pavone;S. G. Young;P. Tontonoz. - In: MOLECULAR AND CELLULAR BIOLOGY. - ISSN 0270-7306. - STAMPA. - 33:(2013), pp. 1503-1514. [10.1128/MCB.01716-12]
IDOL Stimulates Clathrin-Independent Endocytosis and Multivesicular Body-Mediated Lysosomal Degradation of the Low-Density Lipoprotein Receptor
PAVONE, FRANCESCO SAVERIO;
2013
Abstract
The low-density lipoprotein receptor (LDLR) is a critical determinant of plasma cholesterol levels that internalizes lipoprotein cargo via clathrin-mediated endocytosis. Here, we show that the E3 ubiquitin ligase IDOL stimulates a previously unrecognized, clathrin-independent pathway for LDLR internalization.
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