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

10.6K
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...
10.6K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.5K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
2.5K
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

19.9K
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
19.9K
Protein Folding01:22

Protein Folding

118.2K
Overview
118.2K
Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

2.3K
Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
2.3K
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

7.3K
The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
7.3K

You might also read

Related Articles

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

Sort by
Same author

Network Formation Dynamics in Thiol-ene Crosslinked Hyaluronic Acid Hydrogels: Design Principles for In Vitro Tissue Models.

bioRxiv : the preprint server for biology·2026
Same author

Enzymatic Methods for Assembling and Modifying Hydrogel Biomaterials.

Regenerative engineering and translational medicine·2026
Same author

A robust and user-agnostic step-emulsion platform for scalable microgel fabrication.

bioRxiv : the preprint server for biology·2026
Same author

De novo design of protein nanoparticles with integrated functional motifs.

bioRxiv : the preprint server for biology·2026
Same author

Suspended Tissue Engineering with Assemblable Microfluidics (STEAM).

bioRxiv : the preprint server for biology·2025
Same author

Boolean Logic-Based Controlled Release of Bioactive Proteins with Diversified Inputs.

Angewandte Chemie (International ed. in English)·2025

Related Experiment Video

Updated: Jul 5, 2025

Author Spotlight: Photo Switchable Protein Recruitment for Reversible Patterning in Artificial Cellular Systems
07:10

Author Spotlight: Photo Switchable Protein Recruitment for Reversible Patterning in Artificial Cellular Systems

Published on: February 23, 2024

1.2K

Irreversible light-activated SpyLigation mediates split-protein assembly in 4D.

Brizzia G Munoz-Robles1,2, Cole A DeForest3,4,5,6,7,8

  • 1Department of Bioengineering, University of Washington, Seattle, WA, USA.

Nature Protocols
|January 22, 2024
PubMed
Summary

Light-activated SpyLigation (LASL) enables precise control over split-protein assembly. This new method offers rapid, irreversible protein ligation for applications in biomaterials and intracellular studies.

More Related Videos

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
08:34

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

6.8K
Split-BioID — Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment
09:02

Split-BioID — Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment

Published on: April 20, 2018

19.8K

Related Experiment Videos

Last Updated: Jul 5, 2025

Author Spotlight: Photo Switchable Protein Recruitment for Reversible Patterning in Artificial Cellular Systems
07:10

Author Spotlight: Photo Switchable Protein Recruitment for Reversible Patterning in Artificial Cellular Systems

Published on: February 23, 2024

1.2K
OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
08:34

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

6.8K
Split-BioID — Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment
09:02

Split-BioID — Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment

Published on: April 20, 2018

19.8K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biotechnology

Background:

  • Conditional assembly of split-protein pairs is crucial for modulating biological activity.
  • Current methods for protein reconstitution lack spatial/temporal control and specificity.

Purpose of the Study:

  • To develop a light-activated system for precise and irreversible assembly of split-protein pairs.
  • To introduce a method with enhanced spatial and temporal control over protein reconstitution.

Main Methods:

  • Developed light-activated SpyLigation (LASL) using a photoactivatable SpyCatcher (pSC) with a caged lysine.
  • Utilized near-ultraviolet or pulsed near-infrared irradiation to trigger covalent SpyTag (ST)/SpyCatcher (SC) ligation.
  • Incorporated LASL into engineered biomaterials and for intracellular applications.

Main Results:

  • LASL enables rapid and irreversible assembly of split-protein pairs in solution, biomaterials, and intracellularly.
  • Demonstrated efficient synthesis of photocaged amino acids and LASL plasmid design for protein expression.
  • Established chemoenzymatic schemes for bioorthogonal handle attachment, enabling patterned protein activation.

Conclusions:

  • LASL provides a powerful tool for conditional protein assembly with high spatial and temporal control.
  • The irreversibility of LASL allows for fast photolithographic patterning without sustained light exposure.
  • LASL can be applied to interrogate and modulate cell signaling in diverse biological settings.