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Homo- and heterodimerization of APP family members promotes intercellular adhesion.

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Homo- and heterodimerization of APP family members promotes intercellular adhesion. / Soba, Peter; Eggert, Simone; Wagner, Katja; Zentgraf, Hanswalter; Siehl, Katjuscha; Kreger, Sylvia; Löwer, Alexander; Langer, Andreas; Merdes, Gunter; Paro, Renato; Masters, Colin L; Müller, Ulrike; Kins, Stefan; Beyreuther, Konrad.

In: EMBO J, Vol. 24, No. 20, 20, 2005, p. 3624-3634.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Soba, P, Eggert, S, Wagner, K, Zentgraf, H, Siehl, K, Kreger, S, Löwer, A, Langer, A, Merdes, G, Paro, R, Masters, CL, Müller, U, Kins, S & Beyreuther, K 2005, 'Homo- and heterodimerization of APP family members promotes intercellular adhesion.', EMBO J, vol. 24, no. 20, 20, pp. 3624-3634. <http://www.ncbi.nlm.nih.gov/pubmed/16193067?dopt=Citation>

APA

Soba, P., Eggert, S., Wagner, K., Zentgraf, H., Siehl, K., Kreger, S., Löwer, A., Langer, A., Merdes, G., Paro, R., Masters, C. L., Müller, U., Kins, S., & Beyreuther, K. (2005). Homo- and heterodimerization of APP family members promotes intercellular adhesion. EMBO J, 24(20), 3624-3634. [20]. http://www.ncbi.nlm.nih.gov/pubmed/16193067?dopt=Citation

Vancouver

Soba P, Eggert S, Wagner K, Zentgraf H, Siehl K, Kreger S et al. Homo- and heterodimerization of APP family members promotes intercellular adhesion. EMBO J. 2005;24(20):3624-3634. 20.

Bibtex

@article{6a037c170cab458990a1c966548b65a6,
title = "Homo- and heterodimerization of APP family members promotes intercellular adhesion.",
abstract = "The amyloid precursor protein (APP) plays a central role in Alzheimer's disease, but its physiological function and that of its mammalian paralogs, the amyloid precursor-like proteins 1 and 2 (APLPs), is still poorly understood. APP has been proposed to form dimers, a process that could promote cell adhesion via trans-dimerization. We investigated the dimerization and cell adhesion properties of APP/APLPs and provide evidence that all three paralogs are capable of forming homo- and heterocomplexes. Moreover, we show that trans-interaction of APP family proteins promotes cell-cell adhesion in a homo- and heterotypic fashion and that endogenous APLP2 is required for cell-cell adhesion in mouse embryonic fibroblasts. We further demonstrate interaction of all the three APP family members in mouse brain, genetic interdependence, and molecular interaction of APP and APLPs in synaptically enriched membrane compartments. Together, our results provide evidence that homo- and heterocomplexes of APP/APLPs promote trans-cellular adhesion in vivo.",
keywords = "Animals, Humans, Mice, Protein Structure, Tertiary, Dimerization, Amyloid beta-Protein Precursor/analysis/genetics/*metabolism, *Cell Adhesion, Fibroblasts/metabolism/physiology, Nerve Tissue Proteins/analysis/genetics/*metabolism, Protease Nexins, Protein Interaction Mapping, Receptors, Cell Surface/*metabolism, Synaptic Membranes/chemistry/metabolism, Animals, Humans, Mice, Protein Structure, Tertiary, Dimerization, Amyloid beta-Protein Precursor/analysis/genetics/*metabolism, *Cell Adhesion, Fibroblasts/metabolism/physiology, Nerve Tissue Proteins/analysis/genetics/*metabolism, Protease Nexins, Protein Interaction Mapping, Receptors, Cell Surface/*metabolism, Synaptic Membranes/chemistry/metabolism",
author = "Peter Soba and Simone Eggert and Katja Wagner and Hanswalter Zentgraf and Katjuscha Siehl and Sylvia Kreger and Alexander L{\"o}wer and Andreas Langer and Gunter Merdes and Renato Paro and Masters, {Colin L} and Ulrike M{\"u}ller and Stefan Kins and Konrad Beyreuther",
year = "2005",
language = "English",
volume = "24",
pages = "3624--3634",
journal = "EMBO J",
issn = "0261-4189",
publisher = "NATURE PUBLISHING GROUP",
number = "20",

}

RIS

TY - JOUR

T1 - Homo- and heterodimerization of APP family members promotes intercellular adhesion.

AU - Soba, Peter

AU - Eggert, Simone

AU - Wagner, Katja

AU - Zentgraf, Hanswalter

AU - Siehl, Katjuscha

AU - Kreger, Sylvia

AU - Löwer, Alexander

AU - Langer, Andreas

AU - Merdes, Gunter

AU - Paro, Renato

AU - Masters, Colin L

AU - Müller, Ulrike

AU - Kins, Stefan

AU - Beyreuther, Konrad

PY - 2005

Y1 - 2005

N2 - The amyloid precursor protein (APP) plays a central role in Alzheimer's disease, but its physiological function and that of its mammalian paralogs, the amyloid precursor-like proteins 1 and 2 (APLPs), is still poorly understood. APP has been proposed to form dimers, a process that could promote cell adhesion via trans-dimerization. We investigated the dimerization and cell adhesion properties of APP/APLPs and provide evidence that all three paralogs are capable of forming homo- and heterocomplexes. Moreover, we show that trans-interaction of APP family proteins promotes cell-cell adhesion in a homo- and heterotypic fashion and that endogenous APLP2 is required for cell-cell adhesion in mouse embryonic fibroblasts. We further demonstrate interaction of all the three APP family members in mouse brain, genetic interdependence, and molecular interaction of APP and APLPs in synaptically enriched membrane compartments. Together, our results provide evidence that homo- and heterocomplexes of APP/APLPs promote trans-cellular adhesion in vivo.

AB - The amyloid precursor protein (APP) plays a central role in Alzheimer's disease, but its physiological function and that of its mammalian paralogs, the amyloid precursor-like proteins 1 and 2 (APLPs), is still poorly understood. APP has been proposed to form dimers, a process that could promote cell adhesion via trans-dimerization. We investigated the dimerization and cell adhesion properties of APP/APLPs and provide evidence that all three paralogs are capable of forming homo- and heterocomplexes. Moreover, we show that trans-interaction of APP family proteins promotes cell-cell adhesion in a homo- and heterotypic fashion and that endogenous APLP2 is required for cell-cell adhesion in mouse embryonic fibroblasts. We further demonstrate interaction of all the three APP family members in mouse brain, genetic interdependence, and molecular interaction of APP and APLPs in synaptically enriched membrane compartments. Together, our results provide evidence that homo- and heterocomplexes of APP/APLPs promote trans-cellular adhesion in vivo.

KW - Animals

KW - Humans

KW - Mice

KW - Protein Structure, Tertiary

KW - Dimerization

KW - Amyloid beta-Protein Precursor/analysis/genetics/metabolism

KW - Cell Adhesion

KW - Fibroblasts/metabolism/physiology

KW - Nerve Tissue Proteins/analysis/genetics/metabolism

KW - Protease Nexins

KW - Protein Interaction Mapping

KW - Receptors, Cell Surface/metabolism

KW - Synaptic Membranes/chemistry/metabolism

KW - Animals

KW - Humans

KW - Mice

KW - Protein Structure, Tertiary

KW - Dimerization

KW - Amyloid beta-Protein Precursor/analysis/genetics/metabolism

KW - Cell Adhesion

KW - Fibroblasts/metabolism/physiology

KW - Nerve Tissue Proteins/analysis/genetics/metabolism

KW - Protease Nexins

KW - Protein Interaction Mapping

KW - Receptors, Cell Surface/metabolism

KW - Synaptic Membranes/chemistry/metabolism

M3 - SCORING: Journal article

VL - 24

SP - 3624

EP - 3634

JO - EMBO J

JF - EMBO J

SN - 0261-4189

IS - 20

M1 - 20

ER -