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Related Concept Videos

Rab Cascades01:25

Rab Cascades

Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
Rab Proteins01:14

Rab Proteins

Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
ER Retrieval Pathway01:45

ER Retrieval Pathway

In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...

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Related Experiment Video

Updated: Jun 16, 2026

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain
10:08

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Published on: August 28, 2012

Evidence for dimeric BACE-mediated APP processing.

Shaobo Jin1, Karin Agerman, Karin Kolmodin

  • 1Department of Cell and Molecular Biology, Karolinska Institute, SE-171 77 Stockholm, Sweden.

Biochemical and Biophysical Research Communications
|January 26, 2010
PubMed
Summary
This summary is machine-generated.

Mutating active site aspartic acids in beta-secretase (BACE) inactivated the enzyme. Co-expression of single mutants restored BACE activity, suggesting dimer formation for amyloid precursor protein processing.

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Consensus Brain-derived Protein, Extraction Protocol for the Study of Human and Murine Brain Proteome Using Both 2D-DIGE and Mini 2DE Immunoblotting
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Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification (BiCAP)
06:45

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification (BiCAP)

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Last Updated: Jun 16, 2026

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain
10:08

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Published on: August 28, 2012

Consensus Brain-derived Protein, Extraction Protocol for the Study of Human and Murine Brain Proteome Using Both 2D-DIGE and Mini 2DE Immunoblotting
10:51

Consensus Brain-derived Protein, Extraction Protocol for the Study of Human and Murine Brain Proteome Using Both 2D-DIGE and Mini 2DE Immunoblotting

Published on: April 10, 2014

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification (BiCAP)
06:45

Dissecting Multi-protein Signaling Complexes by Bimolecular Complementation Affinity Purification (BiCAP)

Published on: June 15, 2018

Area of Science:

  • Biochemistry
  • Neuroscience
  • Molecular Biology

Background:

  • Beta-secretase (BACE) is a key enzyme in amyloid precursor protein (APP) processing.
  • BACE is a significant pharmacological target for Alzheimer's disease due to its role in amyloid-beta production.

Purpose of the Study:

  • To investigate the enzymatic function of BACE by mutating its active site residues.
  • To explore the potential for complementation between BACE active site mutants.

Main Methods:

  • Site-directed mutagenesis of aspartic acid residues in the BACE active site.
  • Assessment of BACE enzymatic activity, glycosylation, and subcellular localization.
  • Analysis of APP processing and inhibition by a small molecule BACE inhibitor.

Main Results:

  • Single active site BACE mutants were functionally inactive but retained normal localization and glycosylation.
  • Substitution of both active site aspartic acids resulted in ER-retained, partially glycosylated, inactive BACE.
  • Co-expression of single mutants partially restored APP beta-site cleavage, indicating functional complementation.

Conclusions:

  • BACE active site mutants can form partially functional dimers, restoring APP processing.
  • This complementation suggests a dimeric structure for BACE's enzymatic activity.
  • The restored activity is sensitive to BACE-specific inhibitors, validating the therapeutic target.