[HTML][HTML] BACE1 protein endocytosis and trafficking are differentially regulated by ubiquitination at lysine 501 and the Di-leucine motif in the carboxyl terminus
EL Kang, B Biscaro, F Piazza, G Tesco - Journal of Biological Chemistry, 2012 - ASBMB
β-Site amyloid precursor protein-cleaving enzyme (BACE1) is a membrane-tethered
member of the aspartyl proteases that has been identified as β-secretase. BACE1 is targeted
through the secretory pathway to the plasma membrane and then is internalized to
endosomes. Sorting of membrane proteins to the endosomes and lysosomes is regulated by
the interaction of signals present in their carboxyl-terminal fragment with specific trafficking
molecules. The BACE1 carboxyl-terminal fragment contains a di-leucine sorting signal (495 …
member of the aspartyl proteases that has been identified as β-secretase. BACE1 is targeted
through the secretory pathway to the plasma membrane and then is internalized to
endosomes. Sorting of membrane proteins to the endosomes and lysosomes is regulated by
the interaction of signals present in their carboxyl-terminal fragment with specific trafficking
molecules. The BACE1 carboxyl-terminal fragment contains a di-leucine sorting signal (495 …