The AGR2 interactome

Frederic Delom; M. Aiman Mohtar; Ted Hupp; Delphine Fessart

doi:10.1152/ajpcell.00532.2018

The AGR2 interactome

Frederic Delom, M. Aiman Mohtar, Ted Hupp, Delphine Fessart

Research output: Contribution to journal › Article › peer-review

Abstract / Description of output

The Anterior Gradient-2 (AGR2) is an Endoplasmic Reticulum (ER)-resident protein belonging to the Protein Disulfide Isomerase (PDI) family which mediates the formation of disulfide bonds, and assists the protein quality control in the ER. In addition to its role in proteostasis, extracellular AGR2 is responsible for various cellular effects in many types of cancer, including cell proliferation, survival, and metastasis. Various OMICs approaches have been used to identify AGR2 binding partners and to investigate the functions of AGR2 in the ER and outside the cell. Emerging data showed that AGR2 exists not only as monomer, but it can also form homodimeric structure and thus interact with different partners, yielding different biological outcomes. In this review, we summarize the AGR2 ' interactome' and discuss the pathological and physiological role of such AGR2 interactions.

Original language	English
Journal	American Journal of Physiology: Cell Physiology
Early online date	23 Oct 2019
DOIs	https://doi.org/10.1152/ajpcell.00532.2018
Publication status	E-pub ahead of print - 23 Oct 2019

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https://www.physiology.org/doi/10.1152/ajpcell.00532.2018

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title = "The AGR2 interactome",

abstract = "The Anterior Gradient-2 (AGR2) is an Endoplasmic Reticulum (ER)-resident protein belonging to the Protein Disulfide Isomerase (PDI) family which mediates the formation of disulfide bonds, and assists the protein quality control in the ER. In addition to its role in proteostasis, extracellular AGR2 is responsible for various cellular effects in many types of cancer, including cell proliferation, survival, and metastasis. Various OMICs approaches have been used to identify AGR2 binding partners and to investigate the functions of AGR2 in the ER and outside the cell. Emerging data showed that AGR2 exists not only as monomer, but it can also form homodimeric structure and thus interact with different partners, yielding different biological outcomes. In this review, we summarize the AGR2 ' interactome' and discuss the pathological and physiological role of such AGR2 interactions.",

author = "Frederic Delom and Mohtar, {M. Aiman} and Ted Hupp and Delphine Fessart",

year = "2019",

month = oct,

day = "23",

doi = "10.1152/ajpcell.00532.2018",

language = "English",

journal = "American Journal of Physiology: Cell Physiology",

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T1 - The AGR2 interactome

AU - Delom, Frederic

AU - Mohtar, M. Aiman

AU - Hupp, Ted

AU - Fessart, Delphine

PY - 2019/10/23

Y1 - 2019/10/23

N2 - The Anterior Gradient-2 (AGR2) is an Endoplasmic Reticulum (ER)-resident protein belonging to the Protein Disulfide Isomerase (PDI) family which mediates the formation of disulfide bonds, and assists the protein quality control in the ER. In addition to its role in proteostasis, extracellular AGR2 is responsible for various cellular effects in many types of cancer, including cell proliferation, survival, and metastasis. Various OMICs approaches have been used to identify AGR2 binding partners and to investigate the functions of AGR2 in the ER and outside the cell. Emerging data showed that AGR2 exists not only as monomer, but it can also form homodimeric structure and thus interact with different partners, yielding different biological outcomes. In this review, we summarize the AGR2 ' interactome' and discuss the pathological and physiological role of such AGR2 interactions.

AB - The Anterior Gradient-2 (AGR2) is an Endoplasmic Reticulum (ER)-resident protein belonging to the Protein Disulfide Isomerase (PDI) family which mediates the formation of disulfide bonds, and assists the protein quality control in the ER. In addition to its role in proteostasis, extracellular AGR2 is responsible for various cellular effects in many types of cancer, including cell proliferation, survival, and metastasis. Various OMICs approaches have been used to identify AGR2 binding partners and to investigate the functions of AGR2 in the ER and outside the cell. Emerging data showed that AGR2 exists not only as monomer, but it can also form homodimeric structure and thus interact with different partners, yielding different biological outcomes. In this review, we summarize the AGR2 ' interactome' and discuss the pathological and physiological role of such AGR2 interactions.

U2 - 10.1152/ajpcell.00532.2018

DO - 10.1152/ajpcell.00532.2018

M3 - Article

SN - 0363-6143

JO - American Journal of Physiology: Cell Physiology

JF - American Journal of Physiology: Cell Physiology

ER -

The AGR2 interactome

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