Related Experiment Video
Updated: Aug 4, 2026
06:45
Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
Published on: May 26, 2011
Functional domains in tetraspanin proteins
Christopher S Stipp1, Tatiana V Kolesnikova, Martin E Hemler
1Dana-Farber Cancer Institute and Department of Pathology, Harvard Medical School, Boston, MA 02115, USA.
Trends in Biochemical Sciences
|February 11, 2003
Summary
New research details the structure and function of tetraspanin proteins. Specific regions are linked to protein interactions, homodimerization, and the assembly of the tetraspanin web.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Tetraspanin proteins are key regulators of cell membrane organization and function.
- Understanding tetraspanin structure is crucial for elucidating their roles in various biological processes.
Purpose of the Study:
- To delineate distinct regions of tetraspanin proteins.
- To link specific structural features to their biochemical functions.
- To understand the assembly of the tetraspanin web.
Main Methods:
- Structural analysis of tetraspanin proteins.
- Biochemical assays to determine protein interactions.
- Analysis of post-translational modifications like palmitoylation.
Main Results:
- Five distinct tetraspanin regions have been identified and functionally characterized.
- The extracellular loop mediates protein interactions and homodimerization.
- Transmembrane domains are involved in intra- and inter-molecular interactions for tetraspanin web assembly.
- Palmitoylation in the intracellular juxtamembrane region also contributes to tetraspanin web assembly.
Conclusions:
- Tetraspanin structure directly correlates with its function in protein complex formation.
- The tetraspanin web is a dynamic network assembled through specific molecular interactions.
- Further research into tetraspanin structure-function relationships will advance understanding of cellular processes.
Related Concept Videos
02:26Conservation of Protein Domains Over Different Proteins
Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
01:25Single-pass Transmembrane Proteins
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...
01:18Membrane Domains
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 anterior...
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 anterior...
01:29Insertion of Multi-pass Transmembrane Proteins in the RER
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...
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...
01:30Assembly of Signaling Complexes
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,...