A helix-to-coil transition at the ε-cut site in the transmembrane dimer of the amyloid precursor protein is required for proteolysis
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Summary
Solid-state NMR spectroscopy is used to establish the structural features of the transmembrane and juxtamembrane domains of APP that facilitate proteolysis and shows that the TM domain forms an α-helical homodimer mediated by consecutive GxxxG motifs.
- Type
- article
- Published
- 2009-02-03
- Cited by
- 109
- References
- 34
- OpenAlex
- https://openalex.org/W19164538
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:43076252
Keywords
Art
References
- Characterization of a Presenilin-mediated Amyloid Precursor Protein Carboxyl-terminal Fragment γ
- Fe65 does not stabilize AICD during activation of transcription in a luciferase assay.
- Amyloidogenic Processing but Not Amyloid Precursor Protein (APP) Intracellular C-terminal Domain Production Requires a Precisely Oriented APP Dimer Assembled by Transmembrane GXXXG Motifs*
- Functional gamma‐secretase inhibitors reduce beta‐amyloid peptide levels in brain
- Pain: Moving from Symptom Control toward Mechanism-Specific Pharmacologic Management
- Crystal structure of a rhomboid family intramembrane protease
- The GxxxG motif: a framework for transmembrane helix-helix association.
- Ectodomain Shedding and Intramembrane Cleavage of Mammalian Notch Proteins Are Not Regulated through Oligomerization*
- Phosphorylation-induced structural changes in the amyloid precursor protein cytoplasmic tail detected by NMR.
- 13C–1H dipolar-assisted rotational resonance in magic-angle spinning NMR
- Homodimerization of Amyloid Precursor Protein and Its Implication in the Amyloidogenic Pathway of Alzheimer's Disease*
- Familial Alzheimer's disease mutations inhibit γ‐secretase‐mediated liberation of β‐amyloid precursor protein carboxy‐terminal fragment
- Second-site Cleavage in Sterol Regulatory Element-binding Protein Occurs at Transmembrane Junction as Determined by Cysteine Panning*
- Implications of threonine hydrogen bonding in the glycophorin A transmembrane helix dimer.
- Transient structure of the amyloid precursor protein cytoplasmic tail indicates preordering of structure for binding to cytosolic factors.
- Structure of a Site-2 Protease Family Intramembrane Metalloprotease
- Analysis of transmembrane domain mutants is consistent with sequential cleavage of Notch by γ‐secretase
- Glycine and β‐branched residues support and modulate peptide helicity in membrane environments
- Val-->Ala mutations selectively alter helix-helix packing in the transmembrane segment of phage M13 coat protein.
- A novel epsilon-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing.
Cited by
- Role of the 39-kDa receptor-associated protein (RAP) in Alzheimer's disease
- Familial Alzheimer’s mutations within APPTM increase Aβ42 production by enhancing accessibility of ε-cleavage site
- Increased H-Bond Stability Relates to Altered ε-Cleavage Efficiency and Aβ Levels in the I45T Familial Alzheimer’s Disease Mutant of APP
- Comparable dimerization found in wildtype and familial Alzheimer's disease amyloid precursor protein mutants.
- Analysis by a highly sensitive split luciferase assay of the regions involved in APP dimerization and its impact on processing
- Dimeric structure of transmembrane domain of amyloid precursor protein in micellar environment
- Side-chain to main-chain hydrogen bonding controls the intrinsic backbone dynamics of the amyloid precursor protein transmembrane helix.
- The Cleavage Domain of the Amyloid Precursor Protein Transmembrane Helix Does Not Exhibit Above‐Average Backbone Dynamics
- What is the role of amyloid precursor protein dimerization?
- Structural Biology of Presenilins and Signal Peptide Peptidases*
- Competition Between Homodimerization and Cholesterol Binding to the C99 Domain of the Amyloid Precursor Protein
- Substrate determinants in the C99 juxtamembrane domains differentially affect γ–secretase cleavage specificity and modulator pharmacology
- The Roles of GxxxG Motif and Gamma-Secretase Components in APP Processing
- Molecular determinants and thermodynamics of the amyloid precursor protein transmembrane domain implicated in Alzheimer's disease
- Presenilin Transmembrane Domain 8 Conserved AXXXAXXXG Motifs Are Required for the Activity of the γ-Secretase Complex*
- Chemical Biology, Molecular Mechanism and Clinical Perspective of γ-Secretase Modulators in Alzheimer’s Disease
- Bacterial and cell-free production of APP671-726 containing amyloid precursor protein transmembrane and metal-binding domains
- Characterization of Pterocarpus erinaceus kino extract and its gamma-secretase inhibitory properties.
- Direct Binding of Cholesterol to the Amyloid Precursor Protein: An Important Interaction in Lipid-Alzheimer’s Disease Relationships?
- The Effects of Transmembrane Sequence and Dimerization on Cleavage of the p75 Neurotrophin Receptor by γ-Secretase*
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