Related Experiment Video
Updated: Mar 1, 2026
08:02
Live-cell Imaging of Endocytic Transport using Functionalized Nanobodies in Cultured Cells
Published on: October 17, 2025
1.0K
Monoubiquitylation: a recurrent theme in membrane protein transport
1Department of Biological Regulation, Weizmann Institute of Science, Rehovot, Israel.
The Israel Medical Association Journal : IMAJ
|May 5, 2006
Summary
Monoubiquitylation, a type of protein modification, is key for regulating membrane protein trafficking and endocytosis. This process is vital for cellular function and implicated in diseases.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Polyubiquitylation historically linked to protein degradation via proteasomes.
- Ubiquitin conjugation is a versatile regulatory mechanism.
- Monoubiquitylation plays a critical role in membrane protein trafficking.
Purpose of the Study:
- To explore the regulatory role of monoubiquitylation in membrane protein trafficking.
- To elucidate the mechanisms by which monoubiquitylation influences endocytosis and sorting.
- To investigate the involvement of ubiquitin-binding domains in these processes.
Main Methods:
- Analysis of monoubiquitylation in diverse transmembrane proteins (e.g., EGFR, RTKs).
- Investigation of ubiquitin-binding domains in endocytic adaptor proteins.
- Study of ubiquitin conjugation's role in endocytic complex formation and adaptor inactivation.
Main Results:
- Monoubiquitylation regulates endocytosis of membrane proteins at the plasma membrane.
- It controls sorting of proteins in endosomes for lysosomal/vacuolar delivery.
- Ubiquitin-binding domains mediate interactions between ubiquitylated proteins and the endocytic machinery.
- Monoubiquitylation of adaptors can enhance complex avidity or mediate inactivation.
Conclusions:
- Monoubiquitylation is a crucial regulator of membrane protein trafficking and endocytosis.
- The ubiquitin-endocytosis interface is exploited by pathogens and implicated in diseases like cancer.
- Understanding these pathways is vital for cellular and disease biology.
More Related Videos
Related Concept Videos
01:19Membrane Asymmetry Regulating Transporters
7.7K
Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
7.7K
01:29Insertion of Multi-pass Transmembrane Proteins in the RER
19.1K
The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
19.1K
01:27Post-translational Translocation of Proteins to the RER
7.9K
A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
7.9K
01:44The Significance of Membrane Transport
43.2K
The transport of solutes across the cell membrane is essential for metabolic processes, like maintaining cell size and volume, generating the action potential, exchanging nutrients and gases, etc. Membrane transport can be either passive or active. It can be simple diffusion, facilitated, or mediated transport aided by transport proteins such as transporters and channels.
Transporters facilitate either an active or passive movement of solutes. They can allow a single-molecule transport down its...
Transporters facilitate either an active or passive movement of solutes. They can allow a single-molecule transport down its...
43.2K
01:44Introduction to Membrane Traffic
9.9K
The ER, Golgi apparatus, endosomes, and lysosomes work in tandem to modify, sort, and package proteins and lipids. An integrated membrane trafficking network facilitates the back and forth shuttling of molecules within different organelles in the same cell or across the cell membrane.
The transport of soluble and membrane proteins is mediated by transport vesicles that collect cargo from one cellular compartment and deliver it to another by fusing with the target organelle membrane. The Rab...
The transport of soluble and membrane proteins is mediated by transport vesicles that collect cargo from one cellular compartment and deliver it to another by fusing with the target organelle membrane. The Rab...
9.9K
01:26Insertion of Single-pass Transmembrane Proteins in the RER
18.5K
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...
18.5K