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49
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These experiments were carried out in fibronectin-null mouse fibroblasts to exclude the adhesion effects of endogenously synthesized and subsequently secreted fibronectin. These cells attached but only partially spread on anti-β1 integrin antibody or the cell-binding domain of fibronectin, immobilized on a plate. Efficient spreading and focal adhesion formation was promoted by antibody-mediated clustering of syndecan-4. This process was blocked by the action of the C3 exotransferase, implying that Rho acts downstream of syndecan-4 2810
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Saoncella S., Echtermeyer F., Denhez F., Nowlen J.K., Mosher D.F., Robinson S.D., Hynes R.O., Goetinck P.F. Syndecan-4 signals cooperatively with integrins in a Rho dependent manner in the assembly of focal adhesions and actin stress fibers. Proc Natl Acad Sci USA. 96:1999;2805-2810. These experiments were carried out in fibronectin-null mouse fibroblasts to exclude the adhesion effects of endogenously synthesized and subsequently secreted fibronectin. These cells attached but only partially spread on anti-β1 integrin antibody or the cell-binding domain of fibronectin, immobilized on a plate. Efficient spreading and focal adhesion formation was promoted by antibody-mediated clustering of syndecan-4. This process was blocked by the action of the C3 exotransferase, implying that Rho acts downstream of syndecan-4.
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50
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This paper shows that syndecan-4 binds the catalytic domain of protein kinase C (PKC)α via a region that is non-conserved between family members; no binding is detected between PKC and syndecan-2 in vitro. Importantly, syndecan-4 binding enhances PKCα activity, although the downstream substrates remain, as yet, elusive. This represents the first reported signaling role for a member of the syndecan family
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Oh E.S., Woods A., Couchman J.R. Syndecan-4 proteoglycan regulates the distribution and activity of protein kinase C. J Biol Chem. 272:1997;8133-8136. This paper shows that syndecan-4 binds the catalytic domain of protein kinase C (PKC)α via a region that is non-conserved between family members; no binding is detected between PKC and syndecan-2 in vitro. Importantly, syndecan-4 binding enhances PKCα activity, although the downstream substrates remain, as yet, elusive. This represents the first reported signaling role for a member of the syndecan family.
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This work reconstitutes αvβ3 integrin crosstalk to α5β1 in phagocytes in K562 cells that only express the α5β1 integrin. Ectopic expression of αvβ3 decreases migration of these cells to fibronectin. Functional analysis localizes the regulation to Ser752 of the β3 cytoplasmic domain, a site mutated in Glazmann's Thrombasthenia. Mutation of this site impairs β3 inhibition of calcium/calmodulin-dependent protein kinase II and αvβ3 crosstalk to α5β1
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Blystone S.D., Slater S.E., Williams M.P., Crow M.T., Brown E.J. A molecular mechanism of integrin crosstalk: αvβ3 suppression of calcium/calmodulin-dependent protein kinase II regulates α5β1 function. J Cell Biol. 145:1999;889-897. This work reconstitutes αvβ3 integrin crosstalk to α5β1 in phagocytes in K562 cells that only express the α5β1 integrin. Ectopic expression of αvβ3 decreases migration of these cells to fibronectin. Functional analysis localizes the regulation to Ser752 of the β3 cytoplasmic domain, a site mutated in Glazmann's Thrombasthenia. Mutation of this site impairs β3 inhibition of calcium/calmodulin-dependent protein kinase II and αvβ3 crosstalk to α5β1.
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