@article{f70fe0b0f0fc11dcbee902004c4f4f50,
title = "The calcium binding protein ALG-2 binds and stabilizes Scotin, a p53-inducible gene product localized at the endoplasmic reticulum membrane.",
abstract = "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.",
author = "Ingrid Draeby and Woods, {Yvonne L} and {la Cour}, {Jonas Marstrand} and Jens Mollerup and Jean-Christophe Bourdon and Berchtold, {Martin W}",
note = "Keywords: Animals; Apoptosis Regulatory Proteins; Calcium-Binding Proteins; DNA-Binding Proteins; Endoplasmic Reticulum; Humans; Intracellular Membranes; Membrane Proteins; Mice; NIH 3T3 Cells; Nuclear Proteins; Proteins; Recombinant Fusion Proteins; Transcription Factors; Tumor Suppressor Protein p53",
year = "2007",
doi = "10.1016/j.abb.2007.07.028",
language = "English",
volume = "467",
pages = "87--94",
journal = "Archives of Biochemistry and Biophysics",
issn = "0003-9861",
publisher = "Academic Press",
number = "1",
}