Related Experiment Video
Updated: May 24, 2026
07:07
Evaluation of Protein–Protein Interactions using an On-Membrane Digestion Technique
Published on: July 19, 2019
ESCRT and calpain--old and new relationships
1Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, Japan.
The FEBS Journal
|March 13, 2012
Summary
This review explores the surprising connections between ESCRT proteins and calpains, revealing their roles in cell functions like division and pH sensing. It highlights their evolutionary links, offering new insights into cellular mechanisms.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- The Endosomal Sorting Complexes Required for Transport (ESCRT) machinery and the calpain system are crucial for diverse cellular processes.
- ESCRT proteins are involved in multivesicular body (MVB) formation, viral budding, and cell division.
- The calpain system plays a role in cellular signaling and adaptation.
Discussion:
- This review series investigates the intersection of ESCRT proteins and calpains, highlighting their collaborative roles in cellular functions.
- It examines the ambient pH sensing and adaptation mechanisms involving both ESCRT and calpain systems.
- The physical and evolutionary linkage between calpains and Protein Kinase C and Endocrine Factor (PEF) proteins is explored.
Key Insights:
- ESCRT proteins are essential for MVB formation, virus budding, and cytokinesis.
- ESCRT and calpain systems are involved in sensing and adapting to ambient pH changes.
- A significant evolutionary and physical link exists between calpains and PEF proteins.
Outlook:
- Further research into the synergistic functions of ESCRT and calpains can uncover novel therapeutic targets.
- Understanding the pH-sensing roles of these systems may provide insights into cellular homeostasis.
- Investigating the evolutionary connections can illuminate the fundamental principles of protein system evolution.
Related Concept Videos
01:24Caspases
Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside cells.
01:33Overview of Secretory Vesicles
Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
01:23Catenins
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...
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...
01:29Protein Folding Quality Check in the RER
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
01:45ER Retrieval Pathway
In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
01:16Calmodulin-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,...
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...