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Alternative processing of the amyloid precursor protein family by rhomboid protease RHBDL4.

Paschkowsky, Sandra, Hamzé, Mehdi, Oestereich, Felix, Munter, Lisa Marie·2016·Journal of Biological Chemistry
DOI 10.1074/jbc.m116.753582
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  • RHBDL4, but not RHBDL1, RHBDL2 or RHBDL3, cleaves APP at multiple sites within its ectodomain, generating a ~70 kDa N-terminal fragment and different C-terminal fragments.

    “Recently, Paschkowsky et al. (2016) showed in HEK cells expressing APP695 that RHBDL4 but not RHDBL1, 2 and 3, cleaves at multiple sites within the ectodomain of APP (Figure 1) and APLP1 and APLP2, generating a N-terminal fragment of ∼70 kDa and different C-terminal fragments whose functions are still unknown.”

    From Emerging Alternative Proteinases in APP Metabolism and Alzheimer’s Disease Pathogenesis: A Focus on MT1-MMP and MT5-MMP (2019) · cites this paper as Paschkowsky et al., 2016

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Research works printed but not linked: 41

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Metadata

Authors
Paschkowsky, S., Hamzé, M., Oestereich, F., & Munter, L. M.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2016-10
Volume
291
Issue
42
Pages
21903-21912
ISSN
0021-9258
DOI
10.1074/jbc.m116.753582
Cited by
58
References
5
Language
en
Licence
Funders
  • Natural Sciences and Engineering Research Council of Canada (RGPIN-2015-04645)
  • Canada Foundation of Innovation (32565)
  • Alzheimer Society of Canada (PT-58872)
  • Fonds d'innovation Pfizer-FRQS sur la maladie d'Alzheimer et les maladies apparentáes (31288)

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