Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Rab Proteins

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...

Overview of Secretory Vesicles

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.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...

Rab Cascades

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.

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Preparing Medical Students for Patient Death: A Pilot Curriculum at Texas A&M College of Medicine.

Journal of patient experience·2026

Same author

Severe Obesity Management in a Large Academic Health System: A Retrospective Evaluation of Metabolic Bariatric Surgery Counselling Practices.

Clinical obesity·2026

Same author

A Novel Method to Profile Transcripts Encoding SH2 Domains in the <i>Patiria miniata</i> Mature Egg Transcriptome.

Cells·2024

Same author

A quantum sensing metrology for magnetic memories.

Npj spintronics·2024

Same author

Distributions of easy axes and reversal processes in patterned MRAM arrays.

Scientific reports·2023

Same author

SARS-CoV-2 outbreak among staff and evacuees at Operation Allies Welcome Safe Havens.

Public health nursing (Boston, Mass.)·2023

Search research articles

Related Experiment Video

Updated: Aug 6, 2025

Assay for Adhesion and Agar Invasion in S. cerevisiae

Assay for Adhesion and Agar Invasion in S. cerevisiae

Published on: November 8, 2006

The human RAP1 and GFAPɛ proteins increase γ-secretase activity in a yeast model system.

Mark J Swanson¹, Kelsey N Lewis¹, Robert Carpenter²

¹Department of Biochemistry and Molecular Genetics, Midwestern University, Glendale, AZ 85308, USA.

G3 (Bethesda, Md.)

|March 17, 2023

Summary

The nuclear protein RAP1 interacts with GFAPɛ and presenilin 1 (PS1), enhancing gamma-secretase activity. This study links RAP1 to Alzheimer's disease (AD) pathogenesis.

Keywords:

Saccharomyces cerevisiae Alzheimer's disease GFAPɛ RAP1 TERF2IP amyloid beta γ-secretase

More Related Videos

Characterizing Histone Post-translational Modification Alterations in Yeast Neurodegenerative Proteinopathy Models

Characterizing Histone Post-translational Modification Alterations in Yeast Neurodegenerative Proteinopathy Models

Published on: March 24, 2019

Quantitative Measurement of γ-Secretase-mediated Amyloid Precursor Protein and Notch Cleavage in Cell-based Luciferase Reporter Assay Platforms

Quantitative Measurement of γ-Secretase-mediated Amyloid Precursor Protein and Notch Cleavage in Cell-based Luciferase Reporter Assay Platforms

Published on: January 25, 2018

Related Experiment Videos

Last Updated: Aug 6, 2025

Assay for Adhesion and Agar Invasion in S. cerevisiae

Assay for Adhesion and Agar Invasion in S. cerevisiae

Published on: November 8, 2006

Characterizing Histone Post-translational Modification Alterations in Yeast Neurodegenerative Proteinopathy Models

Characterizing Histone Post-translational Modification Alterations in Yeast Neurodegenerative Proteinopathy Models

Published on: March 24, 2019

Quantitative Measurement of γ-Secretase-mediated Amyloid Precursor Protein and Notch Cleavage in Cell-based Luciferase Reporter Assay Platforms

Quantitative Measurement of γ-Secretase-mediated Amyloid Precursor Protein and Notch Cleavage in Cell-based Luciferase Reporter Assay Platforms

Published on: January 25, 2018

Area of Science:

Neuroscience
Molecular Biology
Genetics

Background:

Alzheimer's disease (AD) is a neurodegenerative disorder characterized by cognitive decline.
Amyloid beta (Aβ) plaques, formed by γ-secretase processing of amyloid precursor protein (APP), are a hallmark of AD.
Mutations in APP, PS1, and PS2 genes are linked to early-onset AD (EOAD).

Purpose of the Study:

To investigate the role of the nuclear protein RAP1 (TERF2IP) in Alzheimer's disease.
To explore the interaction of RAP1 with GFAPɛ and presenilin 1 (PS1).
To determine the effect of RAP1 and GFAPɛ on γ-secretase activity.

Main Methods:

Co-immunoprecipitation assays to detect protein interactions.
Confocal microscopy to visualize protein colocalization in SH-SY5Y cells.
Yeast-based genetic model to assess γ-secretase activity.

Main Results:

RAP1 interacts with GFAPɛ and PS1 in vitro and in human cell extracts.
RAP1, GFAPɛ, and PS1 colocalize in the cytoplasm of human cells.
RAP1 enhances γ-secretase activity, an effect potentiated by GFAPɛ.

Conclusions:

The nuclear protein RAP1 plays an extratelomeric role in the cytoplasm through interactions with GFAPɛ and PS1.
RAP1's modulation of γ-secretase activity suggests a novel link to Alzheimer's disease.
This research identifies RAP1 as a potential factor in age-related cognitive disorders.