Probing the Mint2 Protein-Protein Interaction Network Relevant to the Pathophysiology of Alzheimer's Disease

Thomas M. T. Jensen; Louise Albertsen; Christian R. O. Bartling; Linda M. Haugaard-kedström; Kristian Strømgaard

doi:10.1002/cbic.201800004

Probing the Mint2 Protein-Protein Interaction Network Relevant to the Pathophysiology of Alzheimer's Disease

Thomas M. T. Jensen, Louise Albertsen, Christian R. O. Bartling, Linda M. Haugaard-kedström, Kristian Strømgaard

3 Citations (Scopus)

Abstract

The intracellular adaptor protein Mint2 binds amyloid precursor protein (APP) and presenilin-1, which are both central constituents of the amyloidogenic pathway associated with Alzheimer’s disease (AD). Additional interaction partners have also been suggested for Mint2; several of them are also pertinent to AD pathogenesis. However, no comparative mapping of the Mint2 protein–protein interaction network is available. Here we provide a systematic characterization of seven interaction partners and address their specificities towards the different binding domains of Mint2, which reveal domain-specific and-nonspecific interaction partners. Moreover, we show that the last two C-terminal amino acids of Mint2 are both important for the intramolecular interaction with the PDZ1 domain and for the stability of Mint2.

Original language	English
Journal	ChemBioChem
Volume	19
Issue number	11
Pages (from-to)	1119-1122
Number of pages	4
ISSN	1439-4227
DOIs	https://doi.org/10.1002/cbic.201800004
Publication status	Published - 4 Jun 2018

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10.1002/cbic.201800004

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title = "Probing the Mint2 Protein-Protein Interaction Network Relevant to the Pathophysiology of Alzheimer's Disease",

abstract = "The intracellular adaptor protein Mint2 binds amyloid precursor protein (APP) and presenilin-1, which are both central constituents of the amyloidogenic pathway associated with Alzheimer{\textquoteright}s disease (AD). Additional interaction partners have also been suggested for Mint2; several of them are also pertinent to AD pathogenesis. However, no comparative mapping of the Mint2 protein–protein interaction network is available. Here we provide a systematic characterization of seven interaction partners and address their specificities towards the different binding domains of Mint2, which reveal domain-specific and-nonspecific interaction partners. Moreover, we show that the last two C-terminal amino acids of Mint2 are both important for the intramolecular interaction with the PDZ1 domain and for the stability of Mint2.",

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language = "English",

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T1 - Probing the Mint2 Protein-Protein Interaction Network Relevant to the Pathophysiology of Alzheimer's Disease

AU - Jensen, Thomas M. T.

AU - Albertsen, Louise

AU - Bartling, Christian R. O.

AU - Haugaard-kedström, Linda M.

AU - Strømgaard, Kristian

PY - 2018/6/4

Y1 - 2018/6/4

N2 - The intracellular adaptor protein Mint2 binds amyloid precursor protein (APP) and presenilin-1, which are both central constituents of the amyloidogenic pathway associated with Alzheimer’s disease (AD). Additional interaction partners have also been suggested for Mint2; several of them are also pertinent to AD pathogenesis. However, no comparative mapping of the Mint2 protein–protein interaction network is available. Here we provide a systematic characterization of seven interaction partners and address their specificities towards the different binding domains of Mint2, which reveal domain-specific and-nonspecific interaction partners. Moreover, we show that the last two C-terminal amino acids of Mint2 are both important for the intramolecular interaction with the PDZ1 domain and for the stability of Mint2.

AB - The intracellular adaptor protein Mint2 binds amyloid precursor protein (APP) and presenilin-1, which are both central constituents of the amyloidogenic pathway associated with Alzheimer’s disease (AD). Additional interaction partners have also been suggested for Mint2; several of them are also pertinent to AD pathogenesis. However, no comparative mapping of the Mint2 protein–protein interaction network is available. Here we provide a systematic characterization of seven interaction partners and address their specificities towards the different binding domains of Mint2, which reveal domain-specific and-nonspecific interaction partners. Moreover, we show that the last two C-terminal amino acids of Mint2 are both important for the intramolecular interaction with the PDZ1 domain and for the stability of Mint2.

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DO - 10.1002/cbic.201800004

M3 - Journal article

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VL - 19

SP - 1119

EP - 1122

JO - ChemBioChem

JF - ChemBioChem

IS - 11

ER -

Probing the Mint2 Protein-Protein Interaction Network Relevant to the Pathophysiology of Alzheimer's Disease

Abstract

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