{'fraction_non_alphanumeric': 0.03934426229508197, 'fraction_numerical': 0.036885245901639344, 'mean_word_length': 5.197969543147208, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
PtdIns 4‐kinaseβ and neuronal calcium sensor‐1 co‐localize but may not directly associate in mammalian neurons

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. J. Neurosci. Res. 62:216–224, 2000. © 2000 Wiley‐Liss, Inc.