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Neurosci Bull. 2016 Apr;32(2):171-6. doi: 10.1007/s12264-016-0021-1. Epub 2016 Mar 9.

Yeast Two-Hybrid Screening for Proteins that Interact with the Extracellular Domain of Amyloid Precursor Protein.

Author information

1
State Key Laboratory of Membrane Biology, College of Life Sciences, PKU-IDG/McGovern Institute for Brain Research, Peking University, Beijing, 100871, China.
2
State Key Laboratory of Membrane Biology, College of Life Sciences, PKU-IDG/McGovern Institute for Brain Research, Peking University, Beijing, 100871, China. yanzhang@pku.edu.cn.

Abstract

Alzheimer's disease (AD) is a neurodegenerative disorder in which amyloid β plaques are a pathological characteristic. Little is known about the physiological functions of amyloid β precursor protein (APP). Based on its structure as a type I transmembrane protein, it has been proposed that APP might be a receptor, but so far, no ligand has been reported. In the present study, 9 proteins binding to the extracellular domain of APP were identified using a yeast two-hybrid system. After confirming the interactions in the mammalian system, mutated PLP1, members of the FLRT protein family, and KCTD16 were shown to interact with APP. These proteins have been reported to be involved in Pelizaeus-Merzbacher disease (PMD) and axon guidance. Therefore, our results shed light on the mechanisms of physiological function of APP in AD, PMD, and axon guidance.

KEYWORDS:

Alzheimer’s disease; Amyloid precursor protein; Cell death; Pelizaeus-Merzbacher disease; Yeast two-hybrid screening

PMID:
26960425
PMCID:
PMC5563743
DOI:
10.1007/s12264-016-0021-1
[Indexed for MEDLINE]
Free PMC Article

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