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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Imaging the Intracellular Trafficking of APP with Photoactivatable GFP
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Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

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SorLA complement-type repeat domains protect the amyloid precursor protein against processing.

Arnela Mehmedbasic1, Sofie K Christensen1, Jonas Nilsson2

  • 1From the Lundbeck Foundation Research Center MIND, Danish Research Institute of Translational Neuroscience Nordic-EMBL Partnership (DANDRITE), Department of Biomedicine, Aarhus University, Ole Worms Allé 3, DK-8000 AarhusC, Denmark and.

The Journal of Biological Chemistry
|December 20, 2014
PubMed
Summary
This summary is machine-generated.

SorLA

Keywords:
Alzheimer DiseaseAmyloid Precursor Protein (APP)CR-domainsFingerprint ResiduesGolgiIntracellular TraffickingMembrane ProteinO-GlycosylationSorLA

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Rapid Generation of Amyloid from Native Proteins In vitro
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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Genetics

Background:

  • SorLA is a neuronal sorting receptor linked to Alzheimer disease.
  • SorLA interacts with amyloid precursor protein (APP), reducing amyloid-β generation.
  • The exact molecular mechanisms of SorLA-APP interaction and its effect on APP processing remain unclear.

Purpose of the Study:

  • To elucidate the molecular determinants of SorLA-APP complex formation.
  • To investigate the role of SorLA's complement-type repeat (CR) domains in APP processing.
  • To explore how SorLA influences APP metabolism and O-linked glycosylation.

Main Methods:

  • Generated SorLA variants (CR-domain deletion and mutants) and stable SH-SY5Y cell lines.
  • Utilized co-immunoprecipitation to study SorLA-APP binding.
  • Employed Western blotting and ELISAs to analyze APP processing and glycosylation.

Main Results:

  • The SorLA CR-cluster is crucial for APP interaction; its deletion abrogates protection against APP processing.
  • Mutations in SorLA CR-domains alter APP O-linked glycosylation.
  • SorLA influences APP metabolism via Golgi-mediated post-translational glycosylation.

Conclusions:

  • SorLA's CR-domains are essential for binding APP and modulating its processing.
  • SorLA affects APP metabolism by controlling O-linked glycosylation, offering potential Alzheimer disease therapeutic targets.
  • Understanding SorLA-APP interactions provides insights into Alzheimer disease pathogenesis and amyloidogenesis.