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

TY - JOUR

T1 - The calcium binding protein ALG-2 binds and stabilizes Scotin, a p53-inducible gene product localized at the endoplasmic reticulum membrane.

AU - Draeby, Ingrid

AU - Woods, Yvonne L

AU - la Cour, Jonas Marstrand

AU - Mollerup, Jens

AU - Bourdon, Jean-Christophe

AU - Berchtold, Martin W

N1 - 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

PY - 2007

Y1 - 2007

N2 - 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.

AB - 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.

U2 - 10.1016/j.abb.2007.07.028

DO - 10.1016/j.abb.2007.07.028

M3 - Journal article

C2 - 17889823

SN - 0003-9861

VL - 467

SP - 87

EP - 94

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

IS - 1

ER -