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Related Concept Videos

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
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...
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.
Two...

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Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes
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Modulation of PC1/3 activity by self-interaction and substrate binding.

Akina Hoshino1, Dorota Kowalska, François Jean

  • 1Department of Anatomy and Neurobiology, University of Maryland-Baltimore, 20 Penn Street, HSFII Room S251, Baltimore, Maryland 21201, USA.

Endocrinology
|February 10, 2011
PubMed
Summary
This summary is machine-generated.

Prohormone convertase (PC)1/3 enzyme activity is regulated by its oligomerization and aggregation state. These processes, along with peptide stabilization, control PC1/3 function in peptide hormone biosynthesis.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Prohormone convertase (PC)1/3 is a key enzyme in processing peptide precursors.
  • Understanding PC1/3 regulation is crucial for peptide hormone synthesis.
  • Current knowledge on PC1/3 activity control is limited.

Purpose of the Study:

  • Investigate the regulation of prohormone convertase (PC)1/3 activity.
  • Determine the role of enzyme oligomerization and aggregation in PC1/3 function.
  • Identify factors influencing PC1/3 stability and activity.

Main Methods:

  • Ion exchange chromatography
  • Two-dimensional gel electrophoresis
  • Gel filtration
  • Cross-linking studies

Main Results:

  • PC1/3 exists in multiple ionic forms due to oligomerization and aggregation.
  • Acidic PC1/3 forms include inactive aggregates and active, oligomerized 87-kDa species with latent activity.
  • Basic 66/74-kDa PC1/3 forms showed no latency and were stabilized by substrates or peptides.
  • The 87-kDa PC1/3 homodimer was activated by specific peptides.

Conclusions:

  • Enzyme oligomerization and aggregation significantly impact PC1/3 surface charge and activity.
  • Peptide stabilization and enzyme oligomerization are key regulatory mechanisms for PC1/3.
  • These findings shed light on the control of PC1/3 activity in secretory granules.