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Proteolytic Processing of Low Density Lipoprotein Receptor-related Protein Mediates Regulated Release of Its Intracellular Domain

May, Petra, Reddy, Y. Krishna, Herz, Joachim·2002·Journal of Biological Chemistry
DOI 10.1074/jbc.m201979200
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Crossref · 10.1074/jbc.m201979200

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  • LRP undergoes BACE cleavage, leading ultimately to release of the cytoplasmic domain and translocation to the nucleus.

    “Co-transfection with BACE led to a substantial increase in luciferase activity suggesting that LRP undergoes BACE cleavage, leading ultimately to release of the cytoplasmic domain and translocation to the nucleus (Fig. 9).”

    From The Low Density Lipoprotein Receptor-related Protein (LRP) Is a Novel β-Secretase (BACE1) Substrate (2005) · cites this paper as [28]

    The paper reports release of LRP’s cytoplasmic domain and, in the Abstract, says FE65 can stimulate its translocation into the nucleus under certain conditions. It does not establish BACE cleavage as the initiating step; the Discussion instead identifies furin and metalloproteinase cleavage and implicates a γ-secretase-like activity in tail release. The citing sentence’s BACE co-transfection result is its own finding, not a result attributed to this source. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

  • γ-Secretase cleavage of LRP leads to release of the LRP intracellular domain (LRP-ICD), which can translocate to the nucleus and interact with Tip60.

    “Furthermore, and as with APP, ␥-secretase cleavage of LRP leads to release of the LRP intracellular domain (LRP-ICD), which can translocate to the nucleus and interact with Tip60 (27,28).”

    From The Low Density Lipoprotein Receptor-related Protein (LRP) Is a Novel β-Secretase (BACE1) Substrate (2005) · cites this paper as [28]

    The Abstract reports release of the LRP intracellular domain by a γ-secretase-like activity, and the paper says FE65 can promote its nuclear translocation under certain conditions. It does not establish an LRP-ICD interaction with Tip60: a later passage (indexed as Abstract; page unavailable) raises the possibility that FE65 binding to LRP and recruitment of Tip60 are mutually exclusive, and its reporter assay did not show Tip60-dependent activity. (LLM, conf=0.90)

    Experimental — accuracy not yet measured

  • LRP-ICD translocates to the nucleus and interacts with Fe65 and Tip60.

    “Although LRP-ICD has been shown to translocate to the nucleus and interact with Fe65 and Tip60 (28,47), whether or not it has a transcriptional role under physiological conditions remains unknown.”

    From The Low Density Lipoprotein Receptor-related Protein (LRP) Is a Novel β-Secretase (BACE1) Substrate (2005) · cites this paper as [28]

    The Abstract says that FE65 can stimulate translocation of the LRP tail fragment into the nucleus under certain conditions, and the Discussion says LRP binds FE65. But the Discussion (Fig. 6C) suggests that FE65 binding to the LRP tail and binding to Tip60 are mutually exclusive; it does not show LRP-ICD interacting with Tip60. Page numbers are unavailable in our copy. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

  • LRP is a known γ-substrate.

    “Because LRP is a known ␥-substrate, we hypothesized that it might also be cleaved by ␤-secretase.”

    From The Low Density Lipoprotein Receptor-related Protein (LRP) Is a Novel β-Secretase (BACE1) Substrate (2005) · cites this paper as [28]

  • Co-transfection with BACE substantially increases luciferase activity in the LRP-Gal4/VP16 assay.

    “Co-transfection with BACE led to a substantial increase in luciferase activity suggesting that LRP undergoes BACE cleavage, leading ultimately to release of the cytoplasmic domain and translocation to the nucleus (Fig. 9).”

    From The Low Density Lipoprotein Receptor-related Protein (LRP) Is a Novel β-Secretase (BACE1) Substrate (2005) · cites this paper as [28]

    The Results describe an LRP-Gal4/VP16 luciferase assay, but do not report BACE co-transfection. A search for BACE found only a Discussion passage about β-secretase cleavage of APP, not an effect of BACE on LRP reporter activity. (LLM, conf=0.76)

    Experimental — accuracy not yet measured

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Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 45

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Metadata

Authors
May, P., Reddy, Y. K., & Herz, J.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2002-05
Volume
277
Issue
21
Pages
18736-18743
ISSN
0021-9258
DOI
10.1074/jbc.m201979200
Cited by
260
References
2
Language
en
Licence

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