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Related Concept Videos

Appendicitis01:19

Appendicitis

Appendicitis is an acute inflammatory condition of the vermiform appendix, most commonly caused by obstruction of its lumen. The appendix is a narrow, blind-ended pouch that extends from the cecum, making it particularly prone to obstruction. Causes include fecaliths, lymphoid hyperplasia (often after viral infections), parasites, tumors, or foreign bodies. This obstruction initiates a cascade of pathological changes.Luminal Obstruction and Early InflammationAfter obstruction, normal mucosal...
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Overview of Secretory Vesicles

Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
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Appendicitis-I: Introduction01:22

Appendicitis-I: Introduction

The appendix, a small, narrow, blind tube extending from the inferior part of the cecum, is widely regarded as a vestigial organ, having lost much of its original function through evolution. Despite its diminished role, the appendix can become inflamed, a condition known as appendicitis.
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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...
cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
GPCRs Regulate Adenylyl Cylase Activity01:09

GPCRs Regulate Adenylyl Cylase Activity

Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of cells.
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S655 phosphorylation enhances APP secretory traffic.

Sandra Isabel Vieira1, Sandra Rebelo, Sara Catarina Domingues

  • 1Centro de Biologia Celular, SACS, Universidade de Aveiro, Portugal.

Molecular and Cellular Biochemistry
|April 22, 2009
PubMed
Summary

Phosphorylation of Alzheimer's Amyloid Precursor Protein (APP) at S655 regulates its transport. This finding reveals a new mechanism influencing APP processing and its potential role in Alzheimer's disease pathogenesis.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Neuroscience

Background:

  • Cellular protein phosphorylation is crucial for regulating protein function.
  • Alzheimer's disease is linked to aberrant processing of the Amyloid Precursor Protein (APP).
  • APP phosphorylation influences its intracellular trafficking and processing.

Purpose of the Study:

  • To investigate the functional significance of Amyloid Precursor Protein (APP) phosphorylation at the S655 residue within the cytoplasmic sorting signal (653)YTSI(656).
  • To determine how S655 phosphorylation impacts APP trafficking dynamics, particularly at the Golgi apparatus.
  • To explore the implications of S655 phosphorylation for APP processing, alpha-secretase activity, and Alzheimer's disease.

Main Methods:

  • Utilized APP(695)-GFP phosphomutants to study S655 phosphorylation.
  • Analyzed Golgi dynamics of phosphomimicking and dephosphomimicking S655 mutants.
  • Correlated Golgi vesicular exit and secretory cleavage to soluble APP (sAPP) with S655 phosphorylation status.

Main Results:

  • S655 phosphorylation positively modulates APP secretory traffic.
  • Phosphomimicking and dephosphomimicking S655 mutants displayed distinct Golgi dynamics.
  • Differential Golgi exit and cleavage to sAPP were observed in S655 mutants.

Conclusions:

  • S655 phosphorylation acts as a key signal regulating APP trafficking at the Golgi.
  • This phosphorylation event influences the production of cytoprotective alpha-secretase cleaved sAPP.
  • Understanding S655 phosphorylation offers potential therapeutic insights for Alzheimer's disease.