Functional Consequences of Integrin Gene Mutations in Mice

Bouvard, Daniel; Brakebusch, Cord; Gustafsson, Erika; Aszódi, Attila; Bengtsson, Tommy; Berna, Alejandro; Fässler, Reinhard

doi:10.1161/hh1501.094874

Cited by 214 publications

(156 citation statements)

References 149 publications

(136 reference statements)

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“…[183][184][185] Integrin function is important in multicellular organisms, and targeted deletion of integrin subunits can strongly impair tissue formation. [186] Given their fundamental physiological roles, it is not surpising integrin-mediated adhesion and signaling events are carefully regulated.…”

Section: Receptor Proximitymentioning

confidence: 99%

“…[103,117,186,[201][202][203][204][205][206][207] An illustration of this approach is the use small molecule dimer of GPCR ligand, which has been used to activate neutrophil chemotaxis. Neutrophils are attracted to sites of bacterial infection by byproducts of bacterial protein synthesis, such as N-formyl methionine-containing peptide fragments.…”

Section: 1b G-protein Coupled Receptors (Gpcrs)-gpcrsmentioning

confidence: 99%

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Synthetic Multivalent Ligands as Probes of Signal Transduction

2006

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Cell surface receptors acquire information from the extracellular environment and coordinate intracellular responses. Evidence from biochemical and structural studies indicates that many receptors do not operate as individual entities, but rather as part of higher-order complexes (e.g. dimers and oligomers). Coupling the functions of multiple receptors may endow signaling pathways with the sensitivity and malleability required to govern cellular responses. Moreover, multireceptor signaling complexes may provide a means of spatially segregating otherwise degenerate signaling cascades. Despite the proposed importance of receptor-receptor processes in cellular signaling, questions concerning the mechanisms, extent, and consequences of receptor co-localization and interreceptor communication remain unanswered.Chemical synthesis can provide a variety of compounds with which to address the role of receptor assembly in signal transduction. The focus of this review is one such approach -the use of synthetic multivalent ligands to characterize receptor function. Multivalent ligands can be generated that possess a variety of sizes, shapes, valencies, orientations, and densities of binding elements. Their unique architectures imbue multivalent ligands with the ability to access binding modes not available to monovalent compounds. Multivalent ligands, therefore, are capable of illuminating aspects of inter-receptor processes that are not readily probed using conventional approaches. We suggest that, as focus shifts from investigations of the function of individual proteins and toward the analysis of multi-receptor signaling complexes, multivalent ligands will become even more valuable tools with which to ask sophisticated mechanistic questions. Further, multivalent ligands may provide new opportunities for manipulating receptor systems for the deconvolution of pathways, diagnosis, and, ultimately, the treatment of disease.

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Section: Receptor Proximitymentioning

confidence: 99%

Section: 1b G-protein Coupled Receptors (Gpcrs)-gpcrsmentioning

confidence: 99%

Synthetic Multivalent Ligands as Probes of Signal Transduction

2006

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“…Here, we give a few such examples and also discuss some potential anti-integrin therapeutic strategies. For a more detailed description of integrin knockout phenotypes in mice we refer to some excellent recent reviews [12,13].…”

Section: Integrins In Mammals: Mouse Genetics and Human Diseasesmentioning

confidence: 99%

“…Over the past decade, fly, worm, and mouse genetics have provided insight into the roles of many ECM components, virtually every integrin, and several integrin-associated proteins in the development and maintenance of tissues and in the progression of diseases [12][13][14]. There is evidence for a role of integrins in facilitating the stable anchorage of cells to the ECM but they are also implicated in cell migration and they act in concert with receptors for soluble factors to regulate cell fate decisions, including survival, proliferation, and differentiation.…”

Section: Introductionmentioning

confidence: 99%

Integrins in regulation of tissue development and function

Danen¹,

Sonnenberg²

2003

The Journal of Pathology

231

173

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Cell adhesion is indispensable for embryonic development and for proper tissue function. In metazoans, integrins are the major adhesion receptors that connect cells to components of the extracellular matrix. Integrins are implicated in assembly of extracellular matrices, cell adhesion and migration on extracellular matrices, and in vertebrates (in which the integrin family has expanded) they can also mediate cell-cell adhesion. Furthermore, integrinmediated adhesion can modulate many different signal transduction cascades and support cell survival, proliferation, and influence the expression of differentiation-related genes. In this review we briefly explain how integrins can affect so many different aspects of cell behavior and discuss evidence for roles of integrins in tissue development, function, and disease.

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“…These events contribute in turn to the maintenance of tissue integrity, embryogenesis, wound healing, while their deregulation leads to different types of pathogenesis (Bouvard et al, 2001;Brakebusch and Fassler, 2003). Among the numerous types of adhesion receptors, the integrin family plays an important role, not only by supporting cell adhesion but also by its capability to transmit and/or to modulate cellular signaling (outside-in signaling) by converting extracellular information (such as local concentration of growth factors or the nature of the ECM) into intracellular responses such as cell proliferation, differentiation and apoptosis (Giancotti and Ruoslahti, 1999;Keely et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

Unraveling ICAP-1 function: Toward a new direction?

Bouvard

Millon‐Frémillon

Dupé-Manet

et al. 2006

European Journal of Cell Biology

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Cell adhesion to either the extracellular matrix (ECM) or to neighbouring cells is of critical importance during both physiological and pathological situations. Integrins are a large family of cell adhesion receptors composed of two non-covalently linked α and β sub-units. They have a well identified dual function of mediating both firm adhesion and signalling. The short cytoplasmic domain of integrin can interact with cytoplasmic proteins that are either shared by several different integrins or specific for one type of integrin. ICAP-1 (Integrin Cytoplasmic domain Associated Protein-1) is a small cytoplasmic protein that specifically interacts with the β 1 integrin subunit. In this review we will discuss recent findings on ICAP-1, not only at the structural and functional level, but also its possible interconnection in other signalling pathways such as those that control cell proliferation.

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Functional Consequences of Integrin Gene Mutations in Mice

Cited by 214 publications

References 149 publications

Synthetic Multivalent Ligands as Probes of Signal Transduction

Synthetic Multivalent Ligands as Probes of Signal Transduction

Integrins in regulation of tissue development and function

Unraveling ICAP-1 function: Toward a new direction?

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