Journal article
Laminin-binding integrins and their tetraspanin partners as potential antimetastatic targets
Expert reviews in molecular medicine, Vol.12, pp.e3-e3
01/18/2010
DOI: 10.1017/S1462399409001355
PMCID: PMC2811424
PMID: 20078909
Abstract
Within the integrin family of cell adhesion receptors, integrins alpha3beta1, alpha6beta1, alpha6beta4 and alpha7beta1 make up a laminin-binding subfamily. The literature is divided on the role of these laminin-binding integrins in metastasis, with different studies indicating either pro- or antimetastatic functions. The opposing roles of the laminin-binding integrins in different settings might derive in part from their unusually robust associations with tetraspanin proteins. Tetraspanins organise integrins into multiprotein complexes within discrete plasma membrane domains termed tetraspanin-enriched microdomains (TEMs). TEM association is crucial to the strikingly rapid cell migration mediated by some of the laminin-binding integrins. However, emerging data suggest that laminin-binding integrins also promote the stability of E-cadherin-based cell-cell junctions, and that tetraspanins are essential for this function as well. Thus, TEM association endows the laminin-binding integrins with both pro-invasive functions (rapid migration) and anti-invasive functions (stable cell junctions), and the composition of TEMs in different cell types might help determine the balance between these opposing activities. Unravelling the tetraspanin control mechanisms that regulate laminin-binding integrins will help to define the settings where inhibiting the function of these integrins would be helpful rather than harmful, and may create opportunities to modulate integrin activity in more sophisticated ways than simple functional blockade.
Details
- Title: Subtitle
- Laminin-binding integrins and their tetraspanin partners as potential antimetastatic targets
- Creators
- Christopher S Stipp - Departments of Biology and Molecular Physiology & Biophysics, 210 Iowa Avenue, BBE 236, University of Iowa, Iowa City, IA 52242, USA. christopher-stipp@uiowa.edu
- Resource Type
- Journal article
- Publication Details
- Expert reviews in molecular medicine, Vol.12, pp.e3-e3
- DOI
- 10.1017/S1462399409001355
- PMID
- 20078909
- PMCID
- PMC2811424
- ISSN
- 1462-3994
- eISSN
- 1462-3994
- Grant note
- CA136664 / NCI NIH HHS R01 CA136664 / NCI NIH HHS
- Language
- English
- Date published
- 01/18/2010
- Academic Unit
- Molecular Physiology and Biophysics; Biology
- Record Identifier
- 9984217413702771
Metrics
12 Record Views