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IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and produces two-second...
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G-Protein Gated Ion Channels

GPCRs are primarily responsible for our sense of smell, taste, and vision.  The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
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Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high affinity and are together...
GTPases and their Regulation02:14

GTPases and their Regulation

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G-protein Coupled Receptors

G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.

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Using Microtiter Dish Radiolabeling for Multiple In Vivo Measurements Of Escherichia coli (p)ppGpp Followed by Thin Layer Chromatography
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GULP1 is a novel APP-interacting protein that alters APP processing.

Yan Hao1, Candy Yan Hao, Michael S Perkinton

  • 1Biochemistry Programme, School of Life Sciences, the Chinese University of Hong Kong, Shatin, NT, Hong Kong SAR.

The Biochemical Journal
|April 14, 2011
PubMed
Summary

Researchers discovered that engulfment adaptor protein 1 (GULP1) interacts with the amyloid precursor protein (APP). GULP1 influences APP processing and amyloid-beta (Aβ) production, offering new insights into Alzheimer's disease pathogenesis.

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Construction of Model Lipid Membranes Incorporating G-protein Coupled Receptors (GPCRs)

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Alzheimer's disease (AD) pathogenesis is linked to altered amyloid-beta (Aβ) production from amyloid precursor protein (APP).
  • APP C-terminal domain (APPc)-interacting proteins modulate APP processing, acting cooperatively and competitively.
  • Identifying APPc-binding proteins is crucial for understanding APP processing and AD.

Purpose of the Study:

  • To identify novel proteins interacting with the APP C-terminal domain (APPc).
  • To investigate the role of GULP1 (engulfment adaptor protein 1) in APP processing and Aβ generation.

Main Methods:

  • Yeast two-hybrid system to identify APPc-interacting proteins.
  • Confocal microscopy to assess co-localization of APP and GULP1 in neurons.
  • APP-GAL4 reporter assay to evaluate GULP1's effect on APP processing.

Main Results:

  • GULP1 was identified as a novel APPc-interacting protein.
  • The interaction between GULP1 and APP is mediated by APP's NPTY motif and GULP1's phosphotyrosine-binding (PTB) domain.
  • GULP1 overexpression enhanced APP C-terminal fragments (CTFs) and Aβ generation, while GULP1 knockdown suppressed their production.

Conclusions:

  • GULP1 is a novel APP/APPc-interacting protein.
  • GULP1 significantly influences APP processing and Aβ production.
  • GULP1 represents a potential therapeutic target for modulating Aβ levels in Alzheimer's disease.