Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

GPI Anchoring of Proteins in the ER Membrane01:29

GPI Anchoring of Proteins in the ER Membrane

5.1K
GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
5.1K
Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

16.3K
Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
16.3K
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

10.3K
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...
10.3K
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

4.1K
Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
4.1K
G-protein Coupled Receptors01:21

G-protein Coupled Receptors

131.1K
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.
131.1K
Integrins01:10

Integrins

5.0K
Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
5.0K

You might also read

Related Articles

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

Sort by
Same author

Factors Associated With Menopause Symptoms: A Systematic Review and Meta-Analysis.

BJOG : an international journal of obstetrics and gynaecology·2026
Same author

Revisiting HIV-Associated Wasting: Results from a U.S. Cross-Sectional Survey of Health Care Providers' Knowledge, Attitude, and Current Practices.

AIDS research and human retroviruses·2026
Same author

Dynamic Organellar Mapping in yeast reveals extensive protein localization changes during ER stress.

Nature communications·2025
Same author

Menopause care is neglected and inequitable.

BMJ (Clinical research ed.)·2025
Same author

Benefits of aldosterone receptor antagonism in chronic kidney disease: the BARACK-D RCT.

Health technology assessment (Winchester, England)·2025
Same author

Spatial proteomics identifies a CRTC-dependent viral signaling pathway that stimulates production of interleukin-11.

Cell reports·2025
Same journal

Mechanisms underpinning chromosome structure in metazoans.

Molecular biology of the cell·2026
Same journal

Conserved and Divergent Modes of Substrate Interaction Define Selective Localizations and Functions of a Cdc14 Phosphatase.

Molecular biology of the cell·2026
Same journal

Dimerization of the centriolin-like protein Nud1 governs spindle pole body inheritance in budding yeast.

Molecular biology of the cell·2026
Same journal

Non-muscle Myosin II acts as a negative feedback mediator to control cell contraction dynamics in adherent cells.

Molecular biology of the cell·2026
Same journal

The tetraspanin disc proteins, peripherin-2 and ROM1, facilitate CNG channel localization to the rod outer segment.

Molecular biology of the cell·2026
Same journal

Csf1 facilitates adaptive membrane lipid remodeling linked to ER-plasma membrane contact sites.

Molecular biology of the cell·2026
See all related articles

Related Experiment Video

Updated: Dec 20, 2025

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve
09:13

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve

Published on: June 14, 2017

13.2K

The aftiphilin/p200/gamma-synergin complex.

Jennifer Hirst1, Georg H H Borner, Michael Harbour

  • 1Department of Clinical Biochemistry, Cambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 2XY, United Kingdom.

Molecular Biology of the Cell
|March 11, 2005
PubMed
Summary
This summary is machine-generated.

Aftiphilin, a protein interacting with AP-1 and clathrin, forms a complex with p200a and gamma-synergin. This complex is crucial for protein sorting and vesicle transport, though aftiphilin has unique roles in transferrin recycling.

More Related Videos

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
10:50

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography

Published on: March 9, 2010

17.8K
Proteomics to Identify Proteins Interacting with P2X2 Ligand-Gated Cation Channels
16:36

Proteomics to Identify Proteins Interacting with P2X2 Ligand-Gated Cation Channels

Published on: May 18, 2009

15.1K

Related Experiment Videos

Last Updated: Dec 20, 2025

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve
09:13

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve

Published on: June 14, 2017

13.2K
Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
10:50

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography

Published on: March 9, 2010

17.8K
Proteomics to Identify Proteins Interacting with P2X2 Ligand-Gated Cation Channels
16:36

Proteomics to Identify Proteins Interacting with P2X2 Ligand-Gated Cation Channels

Published on: May 18, 2009

15.1K

Area of Science:

  • Cell biology
  • Protein interactions
  • Molecular mechanisms of intracellular trafficking

Background:

  • Aftiphilin is a newly identified protein with unknown function.
  • It possesses motifs suggesting interaction with AP-1 and clathrin.
  • Its precise role in cellular processes remains to be elucidated.

Purpose of the Study:

  • To investigate the function of aftiphilin.
  • To determine aftiphilin's role in the clathrin-coated vesicle (CCV) machinery.
  • To understand the interaction of aftiphilin with AP-1 and other binding partners.

Main Methods:

  • Immunofluorescence microscopy to assess colocalization.
  • Gel filtration chromatography to analyze protein complexes.
  • Small interfering RNA (siRNA) to knock down protein expression.
  • Analysis of protein missorting and endocytic recycling assays.

Main Results:

  • Aftiphilin binds clathrin via an atypical YQW motif and localizes to CCVs.
  • Aftiphilin forms a stable complex with p200a and gamma-synergin.
  • Depletion of aftiphilin or its complex partners impairs sorting of CD8-furin and cathepsin D.
  • Aftiphilin depletion uniquely affects transferrin recycling, causing rapid peripheral accumulation and recycling.

Conclusions:

  • The aftiphilin/p200a/gamma-synergin complex is a bona fide component of the CCV machinery.
  • This complex generally facilitates AP-1 function in protein sorting.
  • The complex may possess additional functions beyond AP-1 facilitation, as indicated by distinct effects on transferrin recycling.