Related Experiment Video
Updated: Dec 30, 2025
10:49
Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
Published on: March 5, 2017
13.8K
The hidden world of membrane microproteins
1The Heart Institute and Division of Molecular Cardiovascular Biology, Cincinnati Children's Hospital Medical Center, Cincinnati, OH, United States; Department of Pediatrics, University of Cincinnati College of Medicine, Cincinnati, OH, United States.
Experimental Cell Research
|January 25, 2020
Summary
Newly discovered microproteins (MPs) are tiny membrane proteins less than 100 amino acids long. This review highlights their biological activities and potential in membrane biology research.
Area of Science:
- Membrane Biology
- Molecular Biology
- Biochemistry
Background:
- Proteins are essential for cellular processes, with membrane proteins playing critical roles.
- A diverse family of membrane proteins includes newly discovered microproteins (MPs), defined as proteins <100 amino acids.
- MPs originate from small open reading frames (sORFs).
Purpose of the Study:
- This review focuses on membrane-associated microproteins.
- To highlight the significant biological activities of MPs.
- To emphasize the potential of MPs in advancing membrane biology.
Main Methods:
- Literature review of recent discoveries in microprotein research.
- Analysis of studies focusing on membrane-associated microproteins.
- Synthesis of current understanding of MP functions and biogenesis.
Main Results:
- Microproteins represent a newly recognized class of membrane proteins.
- MPs exhibit diverse and important biological functions.
- Small open reading frames are a source of novel protein products.
Conclusions:
- Membrane microproteins are emerging as key players in cellular functions.
- Further research into MPs promises to yield significant insights into membrane biology.
- MPs represent a promising area for future investigation and therapeutic development.
Related Concept Videos
01:09Multi-pass Transmembrane Proteins and β-barrels
6.3K
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
6.3K
01:16Introduction to Membrane Proteins
79.7K
The cell membrane, or plasma membrane, is an ever-changing landscape. It is described as a fluid mosaic where various macromolecules are embedded in the phospholipid bilayer. Among the macromolecules are proteins. The protein content varies across cell types. For example, mitochondrial inner membranes contain ~76% protein content, while myelin contains ~18% protein content. Individual cells contain many types of membrane proteins—red blood cells contain over 50—and different cell...
79.7K
01:25Single-pass Transmembrane Proteins
6.3K
Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
6.3K
01:19Fluid Mosaic Model
15.3K
Scientists identified the plasma membrane in the 1890s and its principal chemical components (lipids and proteins) by 1915. The model for plasma membrane structure, proposed in 1935 by Hugh Davson and James Danielli, was the first model to be widely accepted in the scientific community. The model was based on the plasma membrane's "railroad track" appearance in early electron micrographs. Davson and Danielli theorized that the plasma membrane's structure resembled a sandwich...
15.3K
01:26Insertion of Single-pass Transmembrane Proteins in the RER
16.1K
Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
16.1K
01:18Membrane Domains
6.9K
The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the...
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the...
6.9K