Related Experiment Video
Updated: Mar 15, 2026
17:14
In vivo and in vitro Studies of Adaptor-clathrin Interaction
Published on: January 26, 2011
15.1K
Utilizing clathrin triskelions as carriers for spatially controlled multi-protein display
Michael B Deci1, Scott W Ferguson1, Maixian Liu1
1Department of Pharmaceutical Sciences, School of Pharmacy, University at Buffalo, The State University of New York, Buffalo, NY, 14214, USA.
Biomaterials
|September 15, 2016
Summary
Clathrin triskelions enable controlled display of multiple proteins on nanocarriers. This technology enhances protein stability and offers potential for nanotechnology, drug delivery, and therapeutics.
Area of Science:
- Biotechnology
- Nanotechnology
- Molecular Biology
Background:
- Simultaneous and spatially controlled display of diverse proteins on nanocarriers remains a significant challenge.
- Achieving ordered protein attachment is crucial for developing advanced nanocarrier systems.
Purpose of the Study:
- To investigate clathrin triskelions as a versatile platform for the site-specific display of functional proteins.
- To explore the potential of genetically engineered clathrin binding peptides (CBPs) for ordered protein attachment.
Main Methods:
- Genetically fusing CBPs to fluorescent proteins (mCherry and GFP).
- Loading fusion proteins onto clathrin triskelions via specific binding interactions.
- Validating protein attachment using surface plasmon resonance (SPR) and Förster resonance energy transfer (FRET).
Main Results:
- Demonstrated successful site-specific attachment of mCherry and GFP fusion proteins to clathrin triskelions.
- Quantified binding affinities of CBP-modified proteins to clathrin triskelions.
- Confirmed simultaneous attachment of different protein constructs and observed significantly increased circulating half-lives of attached proteins.
Conclusions:
- Clathrin triskelion technology provides a robust method for multifunctional nanocarrier development.
- This platform facilitates spatially controlled display of proteins and peptides.
- Potential applications span nanotechnology, drug delivery, vaccine development, and targeted therapies.
Related Concept Videos
01:12Clathrin Coated Vesicles
9.9K
Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
9.9K
01:22Protein Transport to the Thylakoids
3.1K
Thylakoids are membrane-bound sac-like structures within the chloroplast that serve as sites for photosynthesis. Thylakoid lumen contains many electron transport proteins and is enclosed by a thylakoid membrane rich in the light-harvesting complex. Proteins targeted to the thylakoids are transported as precursors and are sorted by the general TOC/TIC import pathway. Once the precursor reaches the stroma, stromal processing peptidases remove their transit signal and expose thylakoid signal...
3.1K
01:28Protein Translocation Machinery on the ER Membrane
7.2K
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...
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...
7.2K
01:30Assembly of Signaling Complexes
7.0K
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,...
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
7.0K
01:45Vesicular Tubular Clusters
3.3K
After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
With the help of motor proteins such...
3.3K
01:45Overview of Protein Sorting and Transport
23.3K
Eukaryotic cells have different membrane-bound organelles with distinct protein requirements. The process by which proteins are targeted to a specific organelle is called protein sorting.
Protein sorting can be of two types: signal-based sorting and vesicle-based trafficking. In signal-based sorting, specific amino acid sequences called sorting signals target proteins to the proper location inside the cell either via gated transport or by protein translocation. In gated transport, folded...
Protein sorting can be of two types: signal-based sorting and vesicle-based trafficking. In signal-based sorting, specific amino acid sequences called sorting signals target proteins to the proper location inside the cell either via gated transport or by protein translocation. In gated transport, folded...
23.3K