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The Intracellular Domain of the Low Density Lipoprotein Receptor-related Protein Modulates Transactivation Mediated by Amyloid Precursor Protein and Fe65
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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 [27]
The Discussion says LRP cleavage releases its intracellular domain, which translocates to the nucleus; Fig. 5 reports close interaction with Tip60 there. The Discussion describes γ-secretase as the probable cause of cleavage, so the citing sentence states that mechanism more definitively than the source does. Page numbers are unavailable in our copy. (LLM, conf=0.85)
Experimental — accuracy not yet measuredThe multiple alternative functions assigned to LRP1 in AD complicate interpretation of the available experimental data.
“Likely, the multiple alternative functions assigned to this receptor in AD, including intracellular APP transport (Ulery et al., 2000; Pietrzik et al., 2002), blockade of APP signaling (Kinoshita et al., 2003), or Aβ shunt across the blood-brain-barrier (Deane et al., 2004) complicate interpretation of the available experimental data.”
From The Pro-Neurotrophin Receptor Sortilin Is a Major Neuronal Apolipoprotein E Receptor for Catabolism of Amyloid-β Peptide in the Brain (2013) · cites this paper as Kinoshita et al., 2003
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Kang, D. E., Pietrzik, C. U., Baum, L., Chevallier, N., Merriam, D. E., Kounnas, M. Z., Wagner, S. L., Troncoso, J. C., Kawas, C. H., Katzman, R., et al. (2000) · Journal of Clinical Investigation · doi:10.1172/jci11013 · Cited by 354
Pietrzik, C. U., Busse, T., Merriam, D. E., Weggen, S., & Koo, E. H. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf568 · Cited by 198
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Bu, G. (2009) · Nature Reviews Neuroscience · doi:10.1038/nrn2620 · Cited by 1,168
Shinohara, M., Tachibana, M., Kanekiyo, T., & Bu, G. (2017) · Journal of Lipid Research · doi:10.1194/jlr.r075796 · Cited by 297
The Low Density Lipoprotein Receptor-related Protein (LRP) Is a Novel β-Secretase (BACE1) Substrate
von Arnim, C. A. F., Kinoshita, A., Peltan, I. D., Tangredi, M. M., Herl, L., Lee, B. M., Spoelgen, R., Hshieh, T. T., Ranganathan, S., Battey, F. D., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414248200 · Cited by 258
Self-citationCarlo, A.-S., Gustafsen, C., Mastrobuoni, G., Nielsen, M. S., Burgert, T., Hartl, D., Rohe, M., Nykjaer, A., Herz, J., Heeren, J., et al. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.2425-12.2013 · Cited by 117
The keystone of Alzheimer pathogenesis might be sought in Aβ physiology
Puzzo, D., Gulisano, W., Arancio, O., & Palmeri, A. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2015.08.039 · Cited by 116
BRI2 Interacts with Amyloid Precursor Protein (APP) and Regulates Amyloid β (Aβ) Production
Fotinopoulou, A., Tsachaki, M., Vlavaki, M., Poulopoulos, A., Rostagno, A., Frangione, B., Ghiso, J., & Efthimiopoulos, S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500231200 · Cited by 114
Functional Roles of the Interaction of APP and Lipoprotein Receptors
Pohlkamp, T., Wasser, C. R., & Herz, J. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00054 · Cited by 92
FE65 interaction with the ApoE receptor ApoEr2
Hoe, H.-S., Magill, L. A., Guenette, S., Fu, Z., Vicini, S., & Rebeck, G. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600728200 · Cited by 69
The generation and function of soluble apoE receptors in the CNS
Rebeck, G. W., LaDu, M. J., Estus, S., Bu, G., & Weeber, E. J. (2006) · Molecular Neurodegeneration · doi:10.1186/1750-1326-1-15 · Cited by 66
Metadata
- Authors
- Kinoshita, A., Shah, T., Tangredi, M. M., Strickland, D. K., & Hyman, B. T.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-10
- Volume
- 278
- Issue
- 42
- Pages
- 41182-41188
- ISSN
- 0021-9258
- Cited by
- 90
- References
- 2
- Language
- en
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