Ubiquitin Regulates GGA3-mediated Degradation of BACE1
Open accessAbstract
BACE1 (beta-site amyloid precursor protein-cleaving enzyme 1) is a membrane-tethered member of the aspartyl proteases, essential for the production of beta-amyloid, a toxic peptide that accumulates in the brain of subjects affected by Alzheimer disease. The BACE1 C-terminal fragment contains a DXXLL motif that has been shown to bind the VHS (VPS27, Hrs, and STAM) domain of GGA1-3 (Golgi-localized gamma-ear-containing ARF-binding proteins). GGAs are trafficking molecules involved in the transport of proteins containing the DXXLL signal from the Golgi complex to endosomes. Moreover, GGAs bind ubiquitin and traffic synthetic and endosomal ubiquitinated cargoes to lysosomes. We have previously shown that depletion of GGA3 results in increased BACE1 levels and activity because of impaired lysosomal degradation. Here, we report that the accumulation of BACE1 is rescued by the ectopic expression of GGA3 in H4 neuroglioma cells depleted of GGA3. Accordingly, the overexpression of GGA3 reduces the levels of BACE1 and beta-amyloid. We then established that mutations in the GGA3 VPS27, Hrs, and STAM domain (N91A) or in BACE1 di-leucine motif (L499A/L500A), able to abrogate their binding, did not affect the ability of ectopically expressed GGA3 to rescue BACE1 accumulation in cells depleted of GGA3. Instead, we found that BACE1 is ubiquitinated at lysine 501 and is mainly monoubiquitinated and Lys-63-linked polyubiquitinated. Finally, a GGA3 mutant with reduced ability to bind ubiquitin (GGA3L276A) was unable to regulate BACE1 levels both in rescue and overexpression experiments. These findings indicate that levels of GGA3 tightly and inversely regulate BACE1 levels via interaction with ubiquitin sorting machinery.
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Ubiquitination at lysine 501 in the C-terminus of BACE1 is required for GGA3-mediated lysosomal targeting and degradation of BACE1.
“Ubiquitination at lysine 501 in the C-terminus of BACE1 is required for GGA3-mediated lysosomal targeting and the degradation of BACE1 (29,30).”
From BIN1 regulates BACE1 intracellular trafficking and amyloid-β production (2016) · cites this paper as [30]
Figure 5 and its accompanying results (page not provided) show that Lys-501 is in BACE1’s C-terminus and that the K501R substitution greatly reduces BACE1 ubiquitination. The paper also links GGA3’s ubiquitin-binding ability to regulation of BACE1 levels and discusses lysosomal degradation, but it does not show that ubiquitination specifically at Lys-501 is required for GGA3-mediated lysosomal targeting or degradation. (LLM, conf=0.86)
Experimental — accuracy not yet measuredDepletion of GGA3 resulted in reduced degradation of BACE1 in lysosomes and increased Ab production, similar to Bin1-depleted cells.
“The depletion of GGA3, which recognizes ubiquitinated BACE1, resulted in the reduced degradation of BACE1 in the lysosomes and increased Ab production in a similar manner to that observed in Bin1-depleted cells (30,41).”
From BIN1 regulates BACE1 intracellular trafficking and amyloid-β production (2016) · cites this paper as [30]
GGA3 regulates BACE1 trafficking to lysosomes and modulates BACE1 levels; depletion and overexpression of GGA3 inversely regulate BACE1 levels.
“The Golgi-localized, γ-ear-containing clathrin adaptor ARF binding protein 3 (GGA3) regulates the trafficking of BACE1 to lysosomes, and modulates BACE1 levels through interactions with ubiquitin sorting machinery, where depletion and overexpression of GGA3 inversely regulates BACE1 levels [49, 50].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [50]
Ubiquitination of BACE1 promotes its lysosomal degradation and is impaired in AD.
“ubiquitination of BACE1 promotes its degradation in the lysosome and is impaired in AD (37,38).”
From The β-Secretase BACE1 in Alzheimer’s Disease (2021) · cites this paper as [37]
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- Authors
- Kang, E. L., Cameron, A. N., Piazza, F., Walker, K. R., & Tesco, G.
- Affiliations
- Tufts University (US)
- Corresponding author
- Tesco, Giuseppina
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2010-07
- Volume
- 285
- Issue
- 31
- Pages
- 24108-24119
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC2911305
- OpenAlex
- W2032080482
- Cited by
- 111
- References
- 49
- Citations by year
- 2026: 5 · 2025: 4 · 2024: 3 · 2023: 3 · 2022: 1 · 2021: 2 · 2020: 7 · 2019: 6 · 2018: 5 · 2017: 6 · 2016: 9 · 2015: 9 · 2014: 16 · 2013: 11 · 2012: 12
- FWCI
- 7.37
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- BOA (University of Milano-Bicocca) (submittedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging (R01AG033016, R01AG025952)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- BACE1, GGA3, ubiquitin, protein degradation, lysosomal degradation, dileucine motif, amyloid-beta, Alzheimer's disease, monoubiquitination
- MeSH terms
- Amino Acid Sequence, Animals, Gene Expression Regulation, Golgi Apparatus, Humans, Lysosomes, Molecular Sequence Data, Protein Binding, Endosomes, Signal Transduction, Amyloid beta-Peptides, Aspartic Acid Endopeptidases, Sequence Homology, Amino Acid, Ubiquitin, Adaptor Proteins, Vesicular Transport, Mice, Amyloid Precursor Protein Secretases
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