Related Experiment Video
Updated: May 30, 2026
10:07
High-throughput Measurement of Plasma Membrane Resealing Efficiency in Mammalian Cells
Published on: January 7, 2019
Membrane assembly of the cholesterol-dependent cytolysin pore complex
Eileen M Hotze1, Rodney K Tweten
1Department of Microbiology and Immunology, The University of Oklahoma Sciences Center, Oklahoma City, Oklahoma 73104, USA.
Biochimica Et Biophysica Acta
|August 13, 2011
Summary
Cholesterol-dependent cytolysins (CDCs) are bacterial toxins that form pores in cell membranes. Their assembly involves cholesterol binding, triggering structural changes for pore complex formation.
Area of Science:
- Microbiology
- Biochemistry
- Molecular Biology
Background:
- Cholesterol-dependent cytolysins (CDCs) are secreted by Gram-positive bacteria.
- CDCs are pore-forming toxins implicated in bacterial pathogenesis.
- The assembly mechanism of CDC pore complexes has been extensively studied.
Purpose of the Study:
- To review the molecular mechanism of CDC pore complex assembly.
- To highlight novel features in CDC pore formation.
- To connect CDC pore formation insights to other pore-forming proteins.
Main Methods:
- Review of existing literature on CDC structure and function.
- Analysis of studies detailing CDC monomer assembly.
- Focus on cholesterol's role as a receptor and structural modulator.
Main Results:
- CDCs assemble into large β-barrel pore complexes from soluble monomers.
- Pore formation is critically dependent on membrane cholesterol.
- Cholesterol binding induces significant structural changes in CDC monomers.
Conclusions:
- The assembly of CDC pore complexes involves a cholesterol-mediated conformational change.
- Understanding CDC pore formation provides insights into broader protein pore assembly mechanisms.
- This review contributes to the understanding of protein folding in membranes.
More Related Videos
Related Concept Videos
01:12Clathrin Coated Vesicles
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...
01:21Structure of Porins
Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel precursors...
01:28Assembly of the Lipid Bilayer in the ER
Biological membranes are more than just a barrier separating cell cytoplasm from the outside environment. They are highly dynamic and help maintain the integrity and physiological stability of the cells as well as membrane-bound organelles. Membranes also play vital roles in cell-to-cell and intracellular communication.
A large chunk of any biological membrane is composed of phospholipids. These lipids have a heterogeneous distribution across different subcellular organelles and even between...
A large chunk of any biological membrane is composed of phospholipids. These lipids have a heterogeneous distribution across different subcellular organelles and even between...
01:28Protein 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.
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.
00:59Mechanisms of Membrane Domain Formation
Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
01:12Porin Insertion in the Outer Mitochondrial Membrane
Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...