Intracellular location and cell context-dependent function of protein kinase D

Ulrica Marklund, Kurt Lightfoot, Doreen Cantrell (Lead / Corresponding author)

    Research output: Contribution to journalArticlepeer-review

    68 Citations (Scopus)

    Abstract

    Protein kinase D (PKD) is an antigen receptor-activated serine kinase localized at either the plasma membrane or the cytosol of lymphocytes. To probe PKD function at these different locations, transgenesis was used to target active PKD either to the membrane or cytosol of pre-T cells. In recombinase gene null pre-T cells, membrane and cytosolic active PKD both induced differentiation reminiscent of β selection: downregulation of CD25 and upregulation of CD2 and CD5. Active PKDs also induced pre-T cell proliferation, although this response was not universal to all thymocyte subsets. There were two striking differences between the actions of the differentially localized PKDs. Membrane but not cytosolic PKD could induce expression of CD8 and CD4 in recombinase null mice; cytosolic but not membrane PKD suppressed Vβ to DJβ rearrangements of the TCRβ chain locus in wild-type T cells. PKD function is thus determined by its intracellular location and cell context.

    Original languageEnglish
    Pages (from-to)491-501
    Number of pages11
    JournalImmunity
    Volume19
    Issue number4
    DOIs
    Publication statusPublished - Oct 2003

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