Inside-out integrin signalling

Inside-out integrin signalling

“Of particular in the opinion interest” of cell biologists. Papers “of particular interest” selected, from the previous year’s literature, by the au...

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“Of particular in the opinion

interest” of cell biologists.

Papers “of particular interest” selected, from the previous year’s literature, by the authors of reviews in the section on Cell-to-Cell Contact and Extracellular Matrix in the October 1992 issue of Current Opinion in Cell Biology.

Endothelial cells: adhesion and tight junctions selected by Lee L. Rubin ALE%ELDA SM, MULLERWA, BUCK CA, NEWMANPJ: Molecular and Cellular Properties of PECAM-1 (endoCAM/CDSl): A Novel Vascular Cell-Cell Adhesion Molecule. J Cell Biol 1991, 114:1059-1068. This paper demonstrates the adhesive function of PECAN-1 via transfection of COS and L-cells. Perhaps the most surprising result is that transfected L-cell adhesion is Ca2+-dependent, raising the possibility that PECAM-1 binding is heterophilic. RAUB TJ, KUENTZELSL, SAWADAGA: Permeability of Bovine Brain Microvessel Endothelial Cells In Vz’tm Barrier Tightening by a Factor Released from Astroglioma Cells. E&b Cell Res 1992, 199:330-340. This article describes another cell culture model of the blood-brain barrier in which endothelial cells are induced by factors secreted from Cb-glioma cells. The absolute resistance of the endothelial cell monolayers was not very high, but the system may be quite useful in identifying glia-derived factors that influence blood-brain barrier permeability. ’ CITI S: Protein Kinase: Inhibitors Prevent Junction Dissociation Induced by Low Extracellular Calcium in MDCK Epithelial Cells. J Cell Biol1992, ll7:169-178. This article is relevant ~tounderstanding regulation of tight junction resistance, as it implicates one or more kinases in the process of EGTA-induced changes in epithelial adherens and tight junctions.

Modulators of neuronal migration and neurite growth selected by Josef P. Kapfhammer and Martin E. Schwab LEMMONV, BURDEN SM, PAYNEHR, ELMSLZEGJ, HLUIIN ML: Neurite Growth on Different Substrates: Permissive Versus Instructive Influences and the Role of Adhesive Strength. J Neurosci 1992, 12818-826. A systematic study on the relationship between adhesive strength, neurite outgrowth and fasciculation on substrates composed of naturally occurring cell adhesion molecules and extracellular matrix molecules. Shows that the strength of adhesion between growth cone and neurite has little to do with the rate of outgrowth or the preference of the growth cone for a particular substrate. Challenges models that explain growth cone behavior by differential adhesion.

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VINTNER C: Regulation of Embryonic Cell Adhesion by the Cadherin Cytoplasmic Domain. Cell 1992, 69:225-236. Demonstrates two important aspects of cadherin fun.:tions. First, different cadherins compete for binding of the same intracellular proteins, the catenins. Second, these intracellular interactions are necessary for cadherin function including cell adhesion. TIYERON M-C, BARBONI E, RIVEROFBP, GORMLF( AM, SEELEY JP, GROSVELDF, MORRISR: Selective Inhibitic--1 of Neurite Outgrowth on Mature Astrocytes by Thy. : Glycoprotein. Nature 1992, 355:745-748. Presents the first candidate for a neuronal receptor molecule with a specific inhibitory activity. After transfection of Thy-l, a neuronal cell line showed much reduced outgrowth from astrocytes that had been cultured for extended time periods. This inhibitory effect could be abolished by addition of soluble Thy-l protein to the astrocytes or by antibodies blocking Thy-l function. Inside-out integrin signalling selected by Mark H. Ginsberg, Xiaoping Du and Edward F. Plow HIE%BS‘ ML, JAKESS, STACKERSA, WALIACERW, SPRINGER TA: The Cytoplasmic Domain of the Integrin Lymphocyte Function-Associated Antigen- 1 P-Subunit: Sites Required for Binding to Intercellular Adhesion Molecule-l and the Phorbol Ester-Stimulated Phosphorylation Site. J Eq &fed 1991, 174:1227-1238. Detailed mapping of the sites controlling the adhesive function of a,& and of the phosphorylation site. Establishes that phosphorylation is not required to increase adhesion through this integrin. BEERJH, SPRINGERKT, COLLFXR BS: Immobilized ArgGly-Asp (RGD) Peptides of Varying Lengths as Structural Probes of the Platelet Glycoprotein IIb/IIIa Receptor. Blood 1992, 79117-128. Clever work establishes that the projection of a synthetic peptide above the surface to which it is tethered controls the activation dependence of peptide binding to ant&. HERMANOWSKI-VOSATKA A, VAN ST~UJP JAG, SWIGGARD WJ, WRIGHT SD: Integrin Modulating Factor-l: A Lipid that Alters the Function of Leukocyte Integrins. Cell 1992, 68:341-352. Describes a lipid moiety that is produced by stimulated neutrophils and activates clhIp2. When it is characterized, it could represent a novel mechanism of affinity modulation.

@ 1992 Current Biology