Journal article
Functional domains in tetraspanin proteins
Trends in biochemical sciences (Amsterdam. Regular ed.), Vol.28(2), pp.106-112
02/2003
DOI: 10.1016/s0968-0004(02)00014-2
PMID: 12575999
Abstract
Exciting new findings have emerged about the structure, function and biochemistry of tetraspanin proteins. Five distinct tetraspanin regions have now been delineated linking structural features to specific functions. Within the large extracellular loop of tetraspanins, there is a variable region that mediates specific interactions with other proteins, as well as a more highly conserved region that has been suggested to mediate homodimerization. Within the transmembrane region, the four tetraspanin transmembrane domains are probable sites of both intra- and inter-molecular interactions that are crucial during biosynthesis and assembly of the network of tetraspanin-linked membrane proteins known as the 'tetraspanin web'. In the intracellular juxtamembrane region, palmitoylation of cysteine residues also contributes to tetraspanin web assembly, and the C-terminal cytoplasmic tail region could provide specific functional links to cytoskeletal or signaling proteins.
Details
- Title: Subtitle
- Functional domains in tetraspanin proteins
- Creators
- Christopher S Stipp - Dana-Farber Cancer Institute and Department of Pathology, Harvard Medical School, Boston, MA 02115, USATatiana V KolesnikovaMartin E Hemler
- Resource Type
- Journal article
- Publication Details
- Trends in biochemical sciences (Amsterdam. Regular ed.), Vol.28(2), pp.106-112
- Publisher
- England
- DOI
- 10.1016/s0968-0004(02)00014-2
- PMID
- 12575999
- ISSN
- 0968-0004
- eISSN
- 1362-4326
- Language
- English
- Date published
- 02/2003
- Academic Unit
- Molecular Physiology and Biophysics; Biology
- Record Identifier
- 9983991962402771
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