Journal
MOLECULAR AND CELLULAR NEUROSCIENCE
Volume 19, Issue 2, Pages 175-185Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1006/mcne.2001.1065
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Funding
- NCRR NIH HHS [1 S10 RR0 9145-01] Funding Source: Medline
- NIA NIH HHS [AG 14996] Funding Source: Medline
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BACE (beta-site APP cleaving enzyme) has been recently proposed as the major aspartyl protease displaying 0 secretase activity in neurons. The C-terminal domain of BACE contains a dileucine motif (LL499/500) that can potentially regulate its trafficking and endocytosis, and an adjacent serine, which is a potential phosphorylation site (S498) that could modulate the activity of the LL motif. In this paper we show that S498 is phosphorylated by casein kinase 1 (CKI). Mutating the LL to dialanine (AA) caused an increase in the levels of mature BACE. The LL to AA mutation increased levels of BACE on the cell surface and decreased the internalization of BACE. Mutating the S498 to alanine did not alter levels of cell surface BACE. Mutating either the leucines or the serine did not after the secretion of Abeta. Our data are consistent with a role for the cytoplasmic domain in regulating BACE trafficking and localization.
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