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

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Standard

The calcium binding protein ALG-2 binds and stabilizes Scotin, a p53-inducible gene product localized at the endoplasmic reticulum membrane. / Draeby, Ingrid; Woods, Yvonne L; la Cour, Jonas Marstrand; Mollerup, Jens; Bourdon, Jean-Christophe; Berchtold, Martin W.

I: Archives of Biochemistry and Biophysics, Bind 467, Nr. 1, 2007, s. 87-94.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Draeby, I, Woods, YL, la Cour, JM, Mollerup, J, Bourdon, J-C & Berchtold, MW 2007, 'The calcium binding protein ALG-2 binds and stabilizes Scotin, a p53-inducible gene product localized at the endoplasmic reticulum membrane.', Archives of Biochemistry and Biophysics, bind 467, nr. 1, s. 87-94. https://doi.org/10.1016/j.abb.2007.07.028

APA

Draeby, I., Woods, Y. L., la Cour, J. M., Mollerup, J., Bourdon, J-C., & Berchtold, M. W. (2007). The calcium binding protein ALG-2 binds and stabilizes Scotin, a p53-inducible gene product localized at the endoplasmic reticulum membrane. Archives of Biochemistry and Biophysics, 467(1), 87-94. https://doi.org/10.1016/j.abb.2007.07.028

Vancouver

Draeby I, Woods YL, la Cour JM, Mollerup J, Bourdon J-C, Berchtold MW. The calcium binding protein ALG-2 binds and stabilizes Scotin, a p53-inducible gene product localized at the endoplasmic reticulum membrane. Archives of Biochemistry and Biophysics. 2007;467(1):87-94. https://doi.org/10.1016/j.abb.2007.07.028

Author

Draeby, Ingrid ; Woods, Yvonne L ; la Cour, Jonas Marstrand ; Mollerup, Jens ; Bourdon, Jean-Christophe ; Berchtold, Martin W. / The calcium binding protein ALG-2 binds and stabilizes Scotin, a p53-inducible gene product localized at the endoplasmic reticulum membrane. I: Archives of Biochemistry and Biophysics. 2007 ; Bind 467, Nr. 1. s. 87-94.

Bibtex

@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",

}

RIS

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

VL - 467

SP - 87

EP - 94

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

SN - 0003-9861

IS - 1

ER -

ID: 3137671