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Demonstration of BACE (β-secretase) phosphorylation and its interaction with GGA1 in cells by fluorescence-lifetime imaging microscopy

von Arnim, Christine A. F., Tangredi, Michelle M., Peltan, Ithan D., Lee, Bonny M., Irizarry, Michael C., Kinoshita, Ayae, Hyman, Bradley T.·2004·Journal of Cell Science
DOI 10.1242/jcs.01422
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Abstract

β-Secretase (BACE) carries out the first of two proteolysis steps to generate the amyloid-β peptides that accumulate in the senile plaques in Alzheimer's disease (AD). Because most BACE activity occurs in endosomes, signals regulating its trafficking to these compartments are important to an understanding of AD pathogenesis. A DISLL sequence near the BACE C-terminus mediates binding of BACE to the VHS domains of Golgi-localized γ-ear-containing ARF-binding (GGA) proteins, which are involved in the sorting of proteins to endosomes. Phosphorylation of the motif's serine residue regulates BACE recycling back to the cell surface from early endosomes and enhances the interaction of BACE with GGA proteins in isolated protein assays. We found that BACE phosphorylation influences BACE-GGA interactions in cells using a new fluorescence-resonance-energy-transfer-based assay of protein proximity, fluorescence lifetime imaging. Although serine-phosphorylated BACE was distributed throughout the cell, interaction of GGA1 with the wild-type protein occurred in juxtanuclear compartments. Pseudo-phosphorylated and non-phosphorylated BACE mutants remained localized with GGA1 in the Golgi body, but the latter mutation diminished the two proteins' FRET signal. Because BACE phosphorylated at serine residues can be identified in human brain, these data suggest that serine phosphorylation of BACE is a physiologically relevant post-translational modification that regulates trafficking in the juxtanuclear compartment by interaction with GGA1.

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  • BACE1 interacts with GGA proteins that are involved in the subcellular trafficking of BACE1.

    “BACE1 interacts with Golgi-localized, ␥-ear-containing, ADP ribosylation factor-binding (GGA) proteins that are involved in the subcellular trafficking of BACE1.”

    From GGA1 Is Expressed in the Human Brain and Affects the Generation of Amyloid β-Peptide (2006) · cites this paper as von Arnim et al., 2004

  • In previous studies, no significant differences in APP processing were observed in cells that overexpressed BACE1.

    “However, in previous studies, no significant differences in APP processing were observed in cells that overexpressed BACE1 (von Arnim et al., 2004;He et al., 2005).”

    From GGA1 Is Expressed in the Human Brain and Affects the Generation of Amyloid β-Peptide (2006) · cites this paper as von Arnim et al., 2004

  • GGA proteins interact with the cytoplasmic domain of BACE1 in a phosphorylation-state-dependent manner and regulate the endocytic trafficking of this protease.

    “GGA proteins have been shown to interact with the cytoplasmic domain of BACE1 in a phosphorylation-state-dependent manner and to regulate the endocytic trafficking of this protease (He et al., 2002(He et al., , 2003(He et al., , 2005;;von Arnim et al., 2004;Wahle et al., 2005).”

    From GGA1 Is Expressed in the Human Brain and Affects the Generation of Amyloid β-Peptide (2006) · cites this paper as von Arnim et al., 2004

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Metadata

Authors
von Arnim, C. A. F., Tangredi, M. M., Peltan, I. D., Lee, B. M., Irizarry, M. C., Kinoshita, A., & Hyman, B. T.
Affiliations
Alzheimer Disease Research Laboratory, Massachusetts General Hospital, Harvard Medical School, 114 16th Street, Charlestown, MA 02129, USA
Venue
Journal of Cell Science
Publisher
The Company of Biologists
Published
2004-10-15
Volume
117
Issue
22
Pages
5437-5445
ISSN
  • 1477-9137
  • 0021-9533
DOI
10.1242/jcs.01422
Cited by
83
References
2
Language
en

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