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

Protein Complex Assembly02:41

Protein Complex Assembly

16.5K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
16.5K
Protein Complex Assembly02:41

Protein Complex Assembly

2.5K
2.5K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

6.4K
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,...
6.4K
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

4.2K
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...
4.2K
Mechanism of Lamellipodia Formation01:31

Mechanism of Lamellipodia Formation

3.5K
Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
3.5K
Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

2.6K
Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
2.6K

You might also read

Related Articles

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

Sort by
Same author

Mpi-driven N-glycosylation orchestrates mucin O-glycosylation and intestinal homeostasis.

Nature communications·2026
Same author

PPa1 insufficiency drives lysosomal storage disease and inflammatory macrophage expansion in the bone marrow.

bioRxiv : the preprint server for biology·2026
Same author

Structural insights into GM4951 as a lipid droplet GTPase regulating hepatic lipid metabolism.

Nature communications·2025
Same author

The Rab32-LRMDA-Retriever Complex is a Key Regulator of Intestinal Immune Homeostasis.

bioRxiv : the preprint server for biology·2025
Same author

A hypomorphic Mpi mutation unlocks an in vivo tool for studying global N-glycosylation deficiency.

JCI insight·2025
Same author

GPR45 modulates Gα<sub>s</sub> at primary cilia of the paraventricular hypothalamus to control food intake.

Science (New York, N.Y.)·2025
Same journal

Layered social competition coordinates reproductive hierarchy formation in ants.

bioRxiv : the preprint server for biology·2026
Same journal

Combination epigenetic-targeted therapy increases the immunogenicity of poorly immunogenic sarcomas.

bioRxiv : the preprint server for biology·2026
Same journal

Loss of LanC-like proteins delays post-injury regeneration of aging skeletal muscles.

bioRxiv : the preprint server for biology·2026
Same journal

Integrative Transfer Network: Deep Transfer Learning Across Populations and Prediction Targets.

bioRxiv : the preprint server for biology·2026
Same journal

Confidence-supported label-free metabolic imaging with FPhaS phase autofluorescence microscopy.

bioRxiv : the preprint server for biology·2026
Same journal

Sequence-encoded autoinhibition couples mRNA decapping activity to phase separation.

bioRxiv : the preprint server for biology·2026
See all related articles

Related Experiment Video

Updated: Jan 10, 2026

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

20.3K

The Structural Basis for Pacs1-Wdr37 Complex Assembly and Stability.

Le Xiao, Magdalena Grzemska, Xiong Pi

    Biorxiv : the Preprint Server for Biology
    |November 24, 2025
    PubMed
    Summary
    This summary is machine-generated.

    The Pacs1-Wdr37 complex structure reveals how Pacs1 binds Wdr37, crucial for protein stability. A neurodevelopmental mutation in Pacs1 doesn't break this complex but offers therapeutic targets.

    More Related Videos

    In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes
    10:05

    In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes

    Published on: August 13, 2012

    11.7K
    Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
    09:57

    Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach

    Published on: December 17, 2016

    7.0K

    Related Experiment Videos

    Last Updated: Jan 10, 2026

    Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
    10:01

    Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

    Published on: November 28, 2017

    20.3K
    In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes
    10:05

    In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes

    Published on: August 13, 2012

    11.7K
    Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
    09:57

    Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach

    Published on: December 17, 2016

    7.0K

    Area of Science:

    • Molecular Biology
    • Structural Biology
    • Cell Biology

    Background:

    • Phosphofurin acidic cluster sorting protein 1 (Pacs1) is an adaptor protein involved in intracellular trafficking.
    • Pacs1 forms a complex with WD-repeat protein 37 (Wdr37), essential for lymphocyte homeostasis.
    • A validated structure for Pacs1-containing complexes was previously lacking.

    Purpose of the Study:

    • To determine the cryo-electron microscopy structure of the Pacs1-Wdr37 complex.
    • To elucidate the structural basis of Pacs1-Wdr37 interaction and its implications for protein stability.
    • To investigate the impact of a pathogenic Pacs1 mutation (R203W) on complex formation and disease.

    Main Methods:

    • Cryo-electron microscopy (cryo-EM) to determine the Pacs1-Wdr37 complex structure.
    • Analysis of protein-protein interactions and domain interfaces.
    • Structural homology modeling to identify potential phospholipid binding sites.

    Main Results:

    • The Pacs1-Wdr37 complex structure reveals Pacs1 binds Wdr37 via its furin-binding region (FBR).
    • This interaction is critical for the stability and expression of both Pacs1 and Wdr37.
    • The pathogenic Pacs1 R203W mutation does not disrupt complex formation but affects protein stability, suggesting therapeutic avenues.
    • Pacs1 FBR shows structural homology to synaptotagmin C2 domains, indicating a novel ability to bind phospholipids.

    Conclusions:

    • The study defines the structural basis for Pacs1-Wdr37 complex assembly and stability.
    • Findings provide insights into Pacs1-mediated neurodevelopmental disorders and suggest potential therapeutic strategies.
    • Novel Pacs1 functions in membrane association through phospholipid binding are proposed.