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Lateral organization of membrane proteins: tetraspanins spin their web.
- Source :
-
The Biochemical journal [Biochem J] 2009 May 13; Vol. 420 (2), pp. 133-54. Date of Electronic Publication: 2009 May 13. - Publication Year :
- 2009
-
Abstract
- Despite high expression levels at the plasma membrane or in intracellular vesicles, tetraspanins remain among the most mysterious transmembrane molecules 20 years after their discovery. Several genetic studies in mammals and invertebrates have demonstrated key physiological roles for some of these tetraspanins, in particular in the immune response, sperm-egg fusion, photoreceptor function and the normal function of certain epithelia. Other studies have highlighted their ability to modulate cell migration and metastasis formation. Their role in the propagation of infectious agents has drawn recent attention, with evidence for HIV budding in tetraspanin-enriched plasma membrane domains. Infection of hepatocytic cells by two major pathogens, the hepatitis C virus and the malaria parasite, also requires the tetraspanin CD81. The function of tetraspanins is thought to be linked to their ability to associate with one another and a wealth of other integral proteins, thereby building up an interacting network or 'tetraspanin web'. On the basis of the biochemical dissection of the tetraspanin web and recent analysis of the dynamics of some of its constituents, we propose that tetraspanins tightly regulate transient interactions between a variety of molecules and as such favour the efficient assembly of specialized structures upon proper stimulation.
- Subjects :
- Animals
Humans
Membrane Proteins metabolism
Models, Molecular
Protein Binding
Protein Structure, Secondary
Protein Structure, Tertiary
Receptors, Cell Surface chemistry
Receptors, Cell Surface metabolism
Receptors, Cell Surface physiology
Signal Transduction physiology
Membrane Proteins chemistry
Membrane Proteins physiology
Subjects
Details
- Language :
- English
- ISSN :
- 1470-8728
- Volume :
- 420
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- The Biochemical journal
- Publication Type :
- Academic Journal
- Accession number :
- 19426143
- Full Text :
- https://doi.org/10.1042/BJ20082422