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

Ingrid Draeby, Yvonne L. Woods, Jonas M. la Cour, Jens Mollerup, Jean-Christophe Bourdon, Martin W. Berchtold

    Research output: Contribution to journalArticlepeer-review

    18 Citations (Scopus)

    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. (c) 2007 Elsevier Inc. All rights reserved.

    Original languageEnglish
    Pages (from-to)87-94
    Number of pages8
    JournalArchives of Biochemistry and Biophysics
    Volume467
    Issue number1
    DOIs
    Publication statusPublished - 1 Nov 2007

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