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The expression of different cytoplasmic domains could influence the function of the alpha 6 beta l laminin receptor integrin by affecting the ligand binding characteristics of the integrin or by altering the intracellular interactions between alpha 6 and cytosolic components (i.e.
Cell migration is crucial to embryonic development, tissue remodeling and cancer invasion. To migrate properly, cells must integrate multiple incoming signals. Once committed to migration, they coordinately regulate, both spatially and temporally, surface receptors and cytoskeleton, in order to generate traction and movement (Lauffenburger and Horwitz, 1996). Migration usually occurs over extracellular matrix (ECM), and is accompanied by characteristic morphological changes. Cell protrusions, e.g., filopodia or lamellipodia, are sites where adherence contacts for traction generally are formed. To accomplish forward movement, there must be a balance between the establishment of plasma membrane-ECM adherence contacts at the cell leading edge, and their coordinated, asymmetric release at the cell trailing edge (Huttenlocher et al., 1995). While significant advances have been made in identifying molecules involved in cell migration, molecular mechanisms are poorly defined.
The integrin family is composed of 24 members and approximately ten years ago (2003) we published a book devoted to the nine I domain integrin subunits. In this second edition, I am pleased that most of the original authors have been able to contribute to the updated version. I domain containing integrins include collagen receptors and leukocyte receptors. In 2003 the knockout mouse phenotypes for all of the I domain integrins had not yet been published; they are now, and are summarized and discussed in this edition. Interestingly, a recent 10 integrin mutation in dogs has indicated that collagen-binding integrins in the musculoskeletal system might have much more severe phenotypes in larger animals/humans compared to the mild integrin phenotypes observed in collagen-binding integrin deficient mice. This finding is further discussed in the book. In the cancer field, the microenvironment is taking center stage, and here collagen receptors on fibroblasts are predicted to play important roles in paracrine signaling, in regulating tissue stiffness and matrix remodeling. New technologies, new mouse models in combination with analyses of I integrins in larger animals/humans are thus predicted to increase our knowledge about this group of receptors. With this in mind we look forward to another 10 years of research with I domain integrins.
Cell adhesion plays a central role in development and disease. Cell adhesion to particular ligands can affect cytoskeletal organization and cell polarity, cell proliferation, and gene expression. This book is divided into two parts. The first section provides a discussion of the structure and function of the seven major classes of cell adhesion molecules: integrins, cadherins, selectins, heparan sulfate proteoglycans, the immunoglobulin superfamily, the ADAMs proteins, and transmembrane protein tyrosine phosphatases. The roles of these cell adhesion proteins in important processes such as cell mediated immunity, development and disease are discussed. In the second section, the molecular organization and function of junctional complexes, regions of the cell surface that are highly specialized for cell adhesion, are examined. Junctional complexes are now known to mediate adhesive interactions and contribute to transmembrane signaling events that dramatically influence cell behaviour. The biochemical organization of the adhesive membranes and the molecular mechanisms by which they transmit information to the cell are addressed. Written by contributors among the most prominent in the field, Cell Adhesion covers a wide range of topics in a single volume. It will be a great resource for students, teachers and researchers.