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

Cytoskeletal Linker Proteins - Plakins01:09

Cytoskeletal Linker Proteins - Plakins

Plakins are large proteins with binding domains for microtubules, microfilaments, intermediate filaments, and membrane-associated protein complexes at cell junctions. Plakin functions are evolutionarily conserved and are primarily involved in organizing the different components of the cytoskeleton by crosslinking them to each other and connecting them to the cell-matrix and cell adhesion complexes. They are also known to interact with signal transducers, serve as scaffolds for signaling...
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
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,...
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,...
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Catenins01:23

Catenins

Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the adherens...

You might also read

Related Articles

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

Sort by
Same author

Neuropeptide Y and tuberoinfundibular dopamine activities are altered during lactation: role of prolactin.

Endocrinology·1999
Same author

Blood pressure and heart rate in the ovine fetus: ontogenic changes and effects of fetal adrenalectomy.

The American journal of physiology·1999
Same author

Characteristics of delayed excretion of flavonoids in human urine after administration of Shosaiko-to, a herbal medicine.

Biological & pharmaceutical bulletin·1999
Same author

A long terminal repeat of the human endogenous retrovirus ERV-9 is located in the 5' boundary area of the human beta-globin locus control region.

Genomics·1999
Same author

Evaluation of a mucoadhesive buccal patch for delivery of peptides: in vitro screening of bioadhesion.

Drug development and industrial pharmacy·1999
Same author

A targeted disruption of the murine Brca1 gene causes gamma-irradiation hypersensitivity and genetic instability.

Oncogene·1999

Related Experiment Video

Updated: Jun 27, 2026

Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms
13:40

Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms

Published on: July 7, 2011

Complexins: cytosolic proteins that regulate SNAP receptor function

H T McMahon1, M Missler, C Li

  • 1Howard Hughes Medical Institute, University of Texas Southwestern Medical School, Dallas 75235, USA.

Cell
|October 6, 1995
PubMed
Summary

Complexins are newly discovered proteins that regulate exocytosis by competing with alpha-SNAP for binding to the SNAP receptor complex. These highly conserved proteins play a crucial role in neuronal function.

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

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale
10:50

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale

Published on: March 14, 2019

Related Experiment Videos

Last Updated: Jun 27, 2026

Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms
13:40

Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms

Published on: July 7, 2011

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

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale
10:50

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale

Published on: March 14, 2019

Area of Science:

  • Molecular Biology
  • Neuroscience
  • Protein Interactions

Background:

  • Complexins are a newly identified protein family involved in regulating exocytosis.
  • They exhibit high homology and conservation across species, particularly complexin II.
  • Complexins are primarily found in neurons, co-localizing with key exocytosis machinery components like syntaxin and SNAP-25.

Purpose of the Study:

  • To investigate the binding interactions of complexins within the SNAP receptor complex.
  • To determine the role of complexins in the sequential binding events during exocytosis.
  • To compare complexin binding with that of alpha-SNAP and synaptotagmin.

Main Methods:

  • Analysis of protein-protein interactions within the SNAP receptor complex.
  • Characterization of complexin binding affinities to individual SNAP receptor components and the assembled core complex.
  • Comparative binding studies with alpha-SNAP and synaptotagmin.

Main Results:

  • Complexins bind strongly to the assembled SNAP receptor-core complex (syntaxin, synaptobrevin, SNAP-25).
  • Complexins compete with alpha-SNAP for binding to the core complex.
  • Complexins do not compete with synaptotagmin I for binding, suggesting a distinct regulatory role.

Conclusions:

  • Complexins act as key regulators of the exocytosis machinery.
  • They modulate the sequential assembly and function of the SNAP receptor complex.
  • Complexins fine-tune the interaction dynamics between alpha-SNAP and synaptotagmins in the exocytotic process.