PtdIns 4-kinaseβ and neuronal calcium sensor-1 co-localize but may not directly associate in mammalian neurons

Selena E. Bartlett*, Anna J. Reynolds, Michael Weible, Andreas Jeromin, John Roder, Ian A. Hendry

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    12 Citations (Scopus)

    Abstract

    It was recently demonstrated that the yeast homologue of phosphatidylinositol 4-kinaseβ PIK1 is directly associated with frq1, the yeast homologue of mammalian neuronal calcium sensor-1 (NCS-1) (Hendricks et al., [1999] Nat. Cell Biol. 1:234-241). This was a novel finding and suggests that a calcium binding protein activates and regulates PtdIns 4-kinaseβ. This finding had not been shown in mammalian cells and both PtdIns 4-kinaseβ and NCS-1 have been shown to have important roles in the regulation of exocytotic release associated with neurotransmission. The aims of this study were to determine if PtdIns 4-kinaseβ and NCS-1 directly associate in mammalian neural tissues. We show that the immunostaining pattern for PtdIns 4-kinaseβ and NCS-1 is co-localized throughout the neurites of newborn cultured dorsal root ganglia (DRG) neurons but not in E13 DRG neurons. We then provide biochemical evidence that PtdIns 4-kinaseβ may not be in physical association with NCS-1 in mammalian nervous tissue unlike that previously reported in yeast. (C) 2000 Wiley-Liss, Inc.

    Original languageEnglish
    Pages (from-to)216-224
    Number of pages9
    JournalJournal of Neuroscience Research
    Volume62
    Issue number2
    DOIs
    Publication statusPublished - 15 Oct 2000

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