Regulation of tyrosine kinase activation and granule release through beta-arrestin by CXCRI (Q28145365)

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J D Andrews

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A A Kelvin

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S E Bosinger

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M E DeVries

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L Xu

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T Dobransky

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R D Feldman

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S S Ferguson

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D J Kelvin

Granules and secretory vesicles of the human neutrophil.

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language of work or name

English

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publication date

September 2000

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published in

Nature Immunology

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volume

1

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issue

3

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page(s)

227-33

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cites work

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The src-family protein-tyrosine kinase p59hck is located on the secretory granules in human neutrophils and translocates towards the phagosome during cell activation

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beta-arrestins regulate interleukin-8-induced CXCR1 internalization

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beta-arrestin1 interacts with the catalytic domain of the tyrosine kinase c-SRC. Role of beta-arrestin1-dependent targeting of c-SRC in receptor endocytosis

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Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolae

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The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis

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Regulation of Human Interleukin-8 Receptor A: Identification of a Phosphorylation Site Involved in Modulating Receptor Functions

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Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement

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Intracellular localization of SNAP-23 to endosomal compartments

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Identification of two isoforms of the vesicle-membrane fusion protein SNAP-23 in human neutrophils and HL-60 cells.

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Hck Is Activated by Opsonized Zymosan and A23187 in Distinct Subcellular Fractions of Human Granulocytes

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Exocytosis of neutrophil granulocytes

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Out of the phagocyte or into its phagosome: signalling to secretion.

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Novel association of the src family kinases, hck and c-fgr, with CCR3 receptor stimulation: A possible mechanism for eotaxin-induced human eosinophil chemotaxis

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