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

Yu, You; Li, Yinan; Zhang, Yan

doi:10.1007/s12264-016-0021-1

Cited by 8 publications

(4 citation statements)

References 22 publications

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“…Its major pathological characteristics are the presence of amyloid-b (Ab) plaques and neurofibrillary tangles (NFTs) [2]. The plaques are mainly composed of Ab that is produced by sequential proteolytic cleavage of amyloid precursor protein (APP) by band c-secretases [3,4]. NFTs consist of hyperphosphorylated tau, a multifunctional protein involved in microtubule assembly and stabilization [5,6].…”

Section: Introductionmentioning

confidence: 99%

The Mitochondrion: A Potential Therapeutic Target for Alzheimer’s Disease

Zhao

Yao

et al. 2018

Neurosci. Bull.

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Section: Introductionmentioning

confidence: 99%

The Mitochondrion: A Potential Therapeutic Target for Alzheimer’s Disease

Zhao

Yao

et al. 2018

Neurosci. Bull.

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“…siRNA-mediated knockdown of LRRTM3 leads to a reduction in sAPPβ and β-CTF levels and Aβ secretion in SH-SY5Y cells ( Majercak et al, 2006 ; Lincoln et al, 2013 ), suggesting that LRRTM3 modulates β-cleavage of APP ( Figure 7B i). APP also interacts with FLRT1 and FLRT3 in HEK293T cells ( Yu et al, 2016 ) ( Figure 7B ii). The functional role of this interaction remains unclear.…”

Section: Interactions Of Cams With App and The Role That Cams Play In...mentioning

confidence: 99%

Amyloid precursor protein (APP) and amyloid β (Aβ) interact with cell adhesion molecules: Implications in Alzheimer’s disease and normal physiology

Pfundstein

Nikonenko

Sytnyk

2022

Front. Cell Dev. Biol.

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Alzheimer’s disease (AD) is an incurable neurodegenerative disorder in which dysfunction and loss of synapses and neurons lead to cognitive impairment and death. Accumulation and aggregation of neurotoxic amyloid-β (Aβ) peptides generated via amyloidogenic processing of amyloid precursor protein (APP) is considered to play a central role in the disease etiology. APP interacts with cell adhesion molecules, which influence the normal physiological functions of APP, its amyloidogenic and non-amyloidogenic processing, and formation of Aβ aggregates. These cell surface glycoproteins also mediate attachment of Aβ to the neuronal cell surface and induce intracellular signaling contributing to Aβ toxicity. In this review, we discuss the current knowledge surrounding the interactions of cell adhesion molecules with APP and Aβ and analyze the evidence of the critical role these proteins play in regulating the processing and physiological function of APP as well as Aβ toxicity. This is a necessary piece of the complex AD puzzle, which we should understand in order to develop safe and effective therapeutic interventions for AD.

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“…With all its reliability, comparable to mass spectrometry, the yeast two-hybrid system has additional advantages such as low cost, time savings, and simplicity [ 113 ]. The yeast two-hybrid system has been utilized to detect proteins that interact with the extracellular [ 114 ] and the intracellular cytoplasmic domain of APP [ 115 , 116 ].…”

Section: Yeast As a Model Of Admentioning

confidence: 99%

Alzheimer’s Disease: Significant Benefit from the Yeast-Based Models

Epremyan

Mamaev

Zvyagilskaya

2023

IJMS

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Alzheimer’s disease (AD) is an age-related, multifaceted neurological disorder associated with accumulation of aggregated proteins (amyloid Aβ and hyperphosphorylated tau), loss of synapses and neurons, and alterations in microglia. AD was recognized by the World Health Organization as a global public health priority. The pursuit of a better understanding of AD forced researchers to pay attention to well-defined single-celled yeasts. Yeasts, despite obvious limitations in application to neuroscience, show high preservation of basic biological processes with all eukaryotic organisms and offer great advantages over other disease models due to the simplicity, high growth rates on low-cost substrates, relatively simple genetic manipulations, the large knowledge base and data collections, and availability of an unprecedented amount of genomic and proteomic toolboxes and high-throughput screening techniques, inaccessible to higher organisms. Research reviewed above clearly indicates that yeast models, together with other, more simple eukaryotic models including animal models, C. elegans and Drosophila, significantly contributed to understanding Aβ and tau biology. These models allowed high throughput screening of factors and drugs that interfere with Aβ oligomerization, aggregation and toxicity, and tau hyperphosphorylation. In the future, yeast models will remain relevant, with a focus on creating novel high throughput systems to facilitate the identification of the earliest AD biomarkers among different cellular networks in order to achieve the main goal—to develop new promising therapeutic strategies to treat or prevent the disease.

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

Cited by 8 publications

References 22 publications

The Mitochondrion: A Potential Therapeutic Target for Alzheimer’s Disease

The Mitochondrion: A Potential Therapeutic Target for Alzheimer’s Disease

Amyloid precursor protein (APP) and amyloid β (Aβ) interact with cell adhesion molecules: Implications in Alzheimer’s disease and normal physiology

Alzheimer’s Disease: Significant Benefit from the Yeast-Based Models

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