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PMID:11953314
| Citation |
Marambaud, P, Shioi, J, Serban, G, Georgakopoulos, A, Sarner, S, Nagy, V, Baki, L, Wen, P, Efthimiopoulos, S, Shao, Z, Wisniewski, T and Robakis, NK (2002) A presenilin-1/gamma-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions. EMBO J. 21:1948-56 |
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| Abstract |
E-cadherin controls a wide array of cellular behaviors including cell-cell adhesion, differentiation and tissue development. Here we show that presenilin-1 (PS1), a protein involved in Alzheimer's disease, controls a gamma-secretase-like cleavage of E-cadherin. This cleavage is stimulated by apoptosis or calcium influx and occurs between human E-cadherin residues Leu731 and Arg732 at the membrane-cytoplasm interface. The PS1/gamma-secretase system cleaves both the full-length E-cadherin and a transmembrane C-terminal fragment, derived from a metalloproteinase cleavage after the E-cadherin ectodomain residue Pro700. The PS1/gamma-secretase cleavage dissociates E-cadherins, beta-catenin and alpha-catenin from the cytoskeleton, thus promoting disassembly of the E-cadherin-catenin adhesion complex. Furthermore, this cleavage releases the cytoplasmic E-cadherin to the cytosol and increases the levels of soluble beta- and alpha-catenins. Thus, the PS1/gamma-secretase system stimulates disassembly of the E-cadherin- catenin complex and increases the cytosolic pool of beta-catenin, a key regulator of the Wnt signaling pathway. |
| Links |
PubMed PMC125968 Online version:10.1093/emboj/21.8.1948 |
| Keywords |
Adherens Junctions; Amino Acid Sequence; Amyloid Precursor Protein Secretases; Animals; Aspartic Acid Endopeptidases; Binding Sites; Cadherins/genetics; Cadherins/metabolism; Endopeptidases/metabolism; Humans; Intracellular Fluid; Matrix Metalloproteinases/metabolism; Membrane Proteins/genetics; Membrane Proteins/metabolism; Mice; Mice, Knockout; Molecular Sequence Data; Presenilin-1; Protein Processing, Post-Translational |
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Significance
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| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
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