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

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,...
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Cytoskeletal Accessory Proteins01:13

Cytoskeletal Accessory Proteins

The cytoskeleton is an essential cell component that plays several structural and functional roles. However, the filaments that make up the cytoskeleton cannot function independently and depend on the accessory or ancillary proteins to effectively carry out their function. Accessory proteins associate with cytoskeletal filaments and their monomers, aiding filament formation and function. They also help in the cross-communication among cytoskeletal filaments. Cytoskeletal accessory proteins are...
Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
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...
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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...

You might also read

Related Articles

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

Sort by
Same author

The Extreme Diversity Of Retinal Amacrine Cells Has Deep Evolutionary Roots.

bioRxiv : the preprint server for biology·2026
Same author

Author Correction: Single-cell atlas of the transcriptome and chromatin accessibility in the human retina.

Nature genetics·2026
Same author

Single-cell atlas of the transcriptome and chromatin accessibility in the human retina.

Nature genetics·2026
Same author

Altered proportions of retinal cell types and distinct visual codes in rodents occupying divergent ecological niches.

Current biology : CB·2025
Same author

Core transcription programs controlling injury-induced neurodegeneration of retinal ganglion cells.

Neuron·2024
Same author

Core transcription programs controlling injury-induced neurodegeneration of retinal ganglion cells.

Neuron·2024

Related Experiment Video

Updated: Jun 15, 2026

Detection of In Situ Protein-protein Complexes at the Drosophila Larval Neuromuscular Junction Using Proximity Ligation Assay
10:31

Detection of In Situ Protein-protein Complexes at the Drosophila Larval Neuromuscular Junction Using Proximity Ligation Assay

Published on: January 20, 2015

Synaptic localization and function of Sidekick recognition molecules require MAGI scaffolding proteins.

Masahito Yamagata1, Joshua R Sanes

  • 1Center for Brain Science and Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138, USA.

The Journal of Neuroscience : the Official Journal of the Society for Neuroscience
|March 12, 2010
PubMed
Summary

Sidekick proteins and Dscams are crucial for retinal synapse formation. Their interaction with MAGI scaffolds, like MAGI-1, dictates synaptic localization and laminar targeting, essential for neural circuit development.

More Related Videos

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules
08:15

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules

Published on: October 17, 2014

Detection of Heterodimerization of Protein Isoforms Using an in Situ Proximity Ligation Assay
09:18

Detection of Heterodimerization of Protein Isoforms Using an in Situ Proximity Ligation Assay

Published on: October 20, 2018

Related Experiment Videos

Last Updated: Jun 15, 2026

Detection of In Situ Protein-protein Complexes at the Drosophila Larval Neuromuscular Junction Using Proximity Ligation Assay
10:31

Detection of In Situ Protein-protein Complexes at the Drosophila Larval Neuromuscular Junction Using Proximity Ligation Assay

Published on: January 20, 2015

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules
08:15

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules

Published on: October 17, 2014

Detection of Heterodimerization of Protein Isoforms Using an in Situ Proximity Ligation Assay
09:18

Detection of Heterodimerization of Protein Isoforms Using an in Situ Proximity Ligation Assay

Published on: October 20, 2018

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Biology

Background:

  • Four transmembrane adhesion molecules, Sidekick-1, Sidekick-2, Down's syndrome cell adhesion molecule (Dscam), and Dscam-like, are key regulators of synapse formation in the vertebrate retina.
  • These molecules possess C termini predicted to interact with postsynaptic density (PSD)-95/Discs Large/ZO-1 (PDZ) domains found in synaptic scaffolding proteins.

Purpose of the Study:

  • To identify the specific synaptic scaffolding proteins that bind to Sidekick and Dscam adhesion molecules.
  • To elucidate the role of these interactions in the localization and function of Sidekick-2 in retinal synapse formation.

Main Methods:

  • Identification of binding partners for Sidekicks and Dscams using members of the membrane-associated guanylate kinase with inverted orientation (MAGI) and PSD-95 subfamilies.
  • Experimental manipulation using RNA interference to deplete MAGI-1 and MAGI-2 to assess their impact on Sidekick-2 localization and function.
  • Analysis of synaptic localization and laminar targeting of neural processes in the retina.

Main Results:

  • Members of the MAGI and PSD-95 protein families were identified as binding partners for Sidekicks and Dscams.
  • Sidekick-2's PDZ-binding C terminus is essential for its synaptic localization in photoreceptors and for promoting lamina-specific arborization.
  • Depletion of MAGI-1 disrupts Sidekick-2 synaptic localization in photoreceptors, while MAGI-2 depletion affects Sidekick-2-dependent laminar targeting in retinal ganglion cells and interneurons.

Conclusions:

  • Sidekick and Dscam adhesion molecules interact with MAGI and PSD-95 family proteins at retinal synapses.
  • Sidekick-2's function and localization are dependent on its integration into a MAGI-containing synaptic scaffold.
  • These findings highlight the critical role of MAGI proteins in organizing synaptic structure and function in the vertebrate retina.