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Vol. 9, Issue 4, 715-731, April 1998
1-Integrin Cytoplasmic Subdomains Involved in Dominant
Negative Function
*Department of Genetics, Biology, and Medical Chemistry, University
of Torino, 10126 Torino, Italy;
The Institute of Biology,
University of Palermo, 90133 Palermo, Italy;
§Department
of Biochemistry, American Red Cross, Rockville, MD 20855;
Department of Experimental Pathology, Lund University
S-22285 Lund, Sweden; and
¶School of Biological Sciences,
University of Manchester, M13 9PT Manchester, United Kingdom
1-integrin cytoplasmic domain consists of a membrane
proximal subdomain common to the four known isoforms ("common"
region) and a distal subdomain specific for each isoform
("variable" region). To investigate in detail the role of these
subdomains in integrin-dependent cellular functions, we used
1A and 1B isoforms as well as four mutants lacking the entire
cytoplasmic domain (1TR), the variable region (1COM), or the
common region (1
COM-B and 1COM-A). By expressing these
constructs in Chinese hamster ovary and 1 integrin-deficient
GD25 cells (Wennerberg et al., J Cell Biol 132, 227-238, 1996), we show that 1B, 1COM,
1COM-B, and 1COM-A molecules are unable to support
efficient cell adhesion to matrix proteins. On exposure to
Mn++ ions, however, 1B, but none of the mutants, can
mediate cell adhesion, indicating specific functional properties of
this isoform. Analysis of adhesive functions of transfected cells shows
that 1B interferes in a dominant negative manner with 1A and
3/5 integrins in cell spreading, focal adhesion
formation, focal adhesion kinase tyrosine phosphorylation, and
fibronectin matrix assembly. None of the 1 mutants tested shows this
property, indicating that the dominant negative effect depends on the
specific combination of common and B subdomains, rather than from the
absence of the A subdomain in the 1B isoform.
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