The calcium binding protein ALG-2 binds and stabilizes Scotin, a p53-inducible gene product localized at the endoplasmic reticulum membrane.

ALG-2 (apoptosis linked gene 2 product) is a calcium binding protein for which no clear cellular function has been established. In this study we identified Scotin as a novel ALG-2 target protein containing 6 PXY and 4 PYP repeats, earlier identified in the ALG-2 binding regions of AIP1/ALIX and TSG101, ...
respectively. An in vitro synthesized C-terminal fragment of Scotin bound specifically to immobilized recombinant ALG-2 and tagged ALG-2 and Scotin were shown by immunoprecipitation to interact in MCF7 and U2OS cell lines. Furthermore ALG-2 bound to endogenous Scotin in extracts from mouse NIH3T3 cells. Overexpression of ALG-2 led to accumulation of Scotin in MCF7 and H1299 cells. In vitro and in vivo binding of ALG-2 to Scotin was demonstrated to be strictly calcium dependent indicating a role of this interaction in calcium signaling pathways.
Mesh Terms:
Animals, Apoptosis Regulatory Proteins, Calcium-Binding Proteins, Carrier Proteins, DNA-Binding Proteins, Endoplasmic Reticulum, Endosomal Sorting Complexes Required for Transport, Humans, Intracellular Membranes, Membrane Proteins, Mice, NIH 3T3 Cells, Nuclear Proteins, Proteins, Recombinant Fusion Proteins, Transcription Factors, Tumor Suppressor Protein p53
Arch. Biochem. Biophys.
Date: Nov. 01, 2007
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