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 Citationer (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.

Originalsprog	Engelsk
Tidsskrift	ChemBioChem
Vol/bind	19
Udgave nummer	11
Sider (fra-til)	1119-1122
Antal sider	4
ISSN	1439-4227
DOI	https://doi.org/10.1002/cbic.201800004
Status	Udgivet - 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.",

author = "Jensen, {Thomas M. T.} and Louise Albertsen and Bartling, {Christian R. O.} and Haugaard-kedstr{\"o}m, {Linda M.} and Kristian Str{\o}mgaard",

year = "2018",

month = jun,

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doi = "10.1002/cbic.201800004",

language = "English",

volume = "19",

pages = "1119--1122",

journal = "ChemBioChem",

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TY - JOUR

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.

U2 - 10.1002/cbic.201800004

DO - 10.1002/cbic.201800004

M3 - Journal article

C2 - 29578633

SN - 1439-4227

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

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