Human APP Intracellular Domain Complex with Fe65-PTB2: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
No edit summary
No edit summary
Line 35: Line 35:
== APP and Alzheimer disease ==
== APP and Alzheimer disease ==
Aβ peptides are generated in neuronal secretory vesicles by proteolytic cleavage of the amyloid precursor protein (APP) by proteases, called β-secretase and γ-secretase that cleave at the N-terminus and variant C-termini of Aβ within APP, respectively, resulting in Aβ of 40 or 42 amino acids (Aβ40 and Aβ42, respectively) (Figure 1). Because the N-termini of Aβ40 and Aβ42 are identical, development of inhibitors that reduce cleavage of APP at the β-secretase site are likely to be effective for reducing Aβ peptide forms with alleviation of neurodegeneration and memory deficit. The APP in the vast majority of AD patients possesses the wild-type β-secretase site sequence. <ref>14<ref>
Aβ peptides are generated in neuronal secretory vesicles by proteolytic cleavage of the amyloid precursor protein (APP) by proteases, called β-secretase and γ-secretase that cleave at the N-terminus and variant C-termini of Aβ within APP, respectively, resulting in Aβ of 40 or 42 amino acids (Aβ40 and Aβ42, respectively) (Figure 1). Because the N-termini of Aβ40 and Aβ42 are identical, development of inhibitors that reduce cleavage of APP at the β-secretase site are likely to be effective for reducing Aβ peptide forms with alleviation of neurodegeneration and memory deficit. The APP in the vast majority of AD patients possesses the wild-type β-secretase site sequence. <ref>14<ref>
== References ==
1. Radzimanowski J, Simon B, Sattler M, Beyreuther K, Sinning I, Wild K. (2008) Structure of the intracellular domain of the amyloid precursor protein in complex with Fe65-PTB2. ''Embo Rep.'' v9 pp. 1134-40. [http://www.ncbi.nlm.nih.gov/pubmed/18833287?dopt=Abstract PMID 18833287]
2. Radzimanowski J, Simon B, Sattler M, Beyreuther K, Sinning I, Wild K. (2008) Structure of the intracellular domain of the amyloid precursor protein in complex with Fe65-PTB2. ''Embo Rep.'' v9 pp. 1134-40. [http://www.ncbi.nlm.nih.gov/pubmed/18833287?dopt=Abstract PMID 18833287]
3. Ando K, Iijima KI, Elliott JI, Kirino Y, Suzuki T. Phosphorylation-dependent regulation of the interaction of amyloid precursor protein with Fe65 affects the production of beta-amyloid.J Biol Chem. 2001 Oct 26;276(43):40353-61. Epub 2001 Aug 21. [http://www.ncbi.nlm.nih.gov/pubmed/11517218itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_RVDocSum&ordinalpos=5 PMID: 11517218]
4. Sabo SL, Ikin AF, Buxbaum JD, Greengard P. The Alzheimer amyloid precursor protein (APP) and FE65, an APP-binding protein, regulate cell movement. J Cell Biol. 2001;153:1403–1414. [PubMed Sabo SL, Ikin AF, Buxbaum JD, Greengard P. The Alzheimer amyloid precursor protein (APP) and FE65, an APP-binding protein, regulate cell movement. J Cell Biol. 2001;153:1403–1414. [PubMed PMID: 11425871
5. Sabo SL, Ikin AF, Buxbaum JD, Greengard P. The amyloid precursor protein and its regulatory protein, FE65, in growth cones and synapses in vitro and in vivo. J Neurosci. 2003;23:5407–5415. [PubMed] 12843239
6. "Alzheimer's disease amyloid beta peptide 25-35 inhibits lipid peroxidation as a result of its membrane interactions."
Walter M.F., Mason P.E., Mason R.P.
Biochem. Biophys. Res. Commun. 233:760-764(1997) [PubMed: 9168929] [Abstract]
Cited for: FUNCTION OF BETA-AMYLOID PEPTIDE AS LIPID PEROXIDATION INHIBITOR, MUTAGENESIS OF MET-706.
7. "The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner."
Kimberly W.T., Zheng J.B., Guenette S.Y., Selkoe D.J.
J. Biol. Chem. 276:40288-40292(2001) [PubMed: 11544248] [Abstract]
Cited for: INTERACTION WITH APBB1, FUNCTION, SUBCELLULAR LOCATION.
8. "Direct interaction of soluble human recombinant tau protein with Abeta 1-42 results in tau aggregation and hyperphosphorylation by tau protein kinase II."
Rank K.B., Pauley A.M., Bhattacharya K., Wang Z., Evans D.B., Fleck T.J., Johnston J.A., Sharma S.K.
FEBS Lett. 514:263-268(2002) [PubMed: 11943163] [Abstract]
Cited for: INTERACTION WITH MAPT, FUNCTION.
9. "APP binds DR6 to trigger axon pruning and neuron death via distinct caspases."
Nikolaev A., McLaughlin T., O'Leary D.D.M., Tessier-Lavigne M.
Nature 457:981-989(2009) [PubMed: 19225519] [Abstract]
Cited for: FUNCTION, CLEAVAGE, INTERACTION WITH TNFRSF21.
10. [http://www.ncbi.nlm.nih.gov/protein/NP_001155.1?ordinalpos=1&itool=EntrezSystem2.PEntrez.Sequence.Sequence_ResultsPanel.Sequence_RVDocSum NCBI Reference Sequence: NP_001155.1]
11. http://www.ncbi.nlm.nih.gov/protein/Q9QXJ1.2?ordinalpos=6&itool=EntrezSystem2.PEntrez.Sequence.Sequence_ResultsPanel.Sequence_RVDocSum
12. http://www.ncbi.nlm.nih.gov/protein/Q9QXJ1.2?ordinalpos=6&itool=EntrezSystem2.PEntrez.Sequence.Sequence_ResultsPanel.Sequence_RVDocSum
13. "The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner."
Kimberly W.T., Zheng J.B., Guenette S.Y., Selkoe D.J.
J. Biol. Chem. 276:40288-40292(2001) [PubMed: 11544248] [Abstract]
Cited for: INTERACTION WITH APBB1, FUNCTION, SUBCELLULAR LOCATION.
14. Vivian Hook, Israel Schechter, Hans-Ulrich Demuth, Gregory Hook. Alternative Pathways for Production of Beta-Amyloid Peptides of Alzheimer’s Disease.Biol Chem. 2008 August; 389(8): 993–1006. [http://www.ncbi.nlm.nih.gov:80/pmc/articles/PMC2654319/?tool=pmcentrez PMCID: PMC2654319]


== Further reading ==
== Further reading ==
Retrieved from "https://proteopedia.org/Human_APP_Intracellular_Domain_Complex_with_Fe65-PTB2"