Phosphoinositide 3-OH kinase activates the beta2 integrin adhesion pathway and induces membrane recruitment of cytohesin-1 (Q28272724)

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L Zeitlmann

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P Schilcher

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C Geiger

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J Kolanus

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W Kolanus

Journal of Biological Chemistry

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language of work or name

English

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publication date

12 June 1998

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published in

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volume

273

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page(s)

14853-61

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issue

24

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cites work

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A role for phosphatidylinositol 3-kinase in the regulation of beta 1 integrin activity by the CD2 antigen

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Inducible interaction of integrin alpha 2 beta 1 with calreticulin. Dependence on the activation state of the integrin

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Alpha L beta 2 integrin/LFA-1 binding to ICAM-1 induced by cytohesin-1, a cytoplasmic regulatory molecule

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PH domains: diverse sequences with a common fold recruit signaling molecules to the cell surface

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Constitutive membrane association potentiates activation of Bruton tyrosine kinase

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Phospholipase C delta 1 requires a pleckstrin homology domain for interaction with the plasma membrane

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The Association of the C-Terminal Region of β1ΣII Spectrin to Brain Membranes Is Mediated by a pH Domain, Does Not Require Membrane Proteins, and Coincides with a Inositol-1,4,5 Trisphosphate Binding Site

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The pleckstrin homology domain of Bruton tyrosine kinase interacts with protein kinase C

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Potential sites of PI-3 kinase function in the endocytic pathway revealed by the PI-3 kinase inhibitor, wortmannin

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Direct interaction between protein kinase C theta (PKC theta) and 14-3-3 tau in T cells: 14-3-3 overexpression results in inhibition of PKC theta translocation and function

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