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Analyzed ArfGAP with dual PH domains 1 (ADAP1) using mass spectrometry and found that ADAP1 is phosphorylated at Y364.
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This review highlights the functions of the neuron-specific protein ADAP1 in neuronal differentiation and neurodegenerative diseases, with an overview of structural and biochemical properties of ADAP1. [review]
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SH-SY5Y cells, stably transfected with GFP-tagged-p42(IP4), show an enhanced NRD protein expression already at an earlier time point after retinoic acid stimulation.
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Tubulin potentiates the interaction of the metalloendopeptidase nardilysin with the neuronal scaffold protein p42IP4/centaurin-alpha1 (ADAP1).
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Full-length KIF13B and CENTA1 form heterotetramers that can bind four phosphoinositide molecules in the vesicle and transport it along the microtubule.
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The ARFGAP domain of p42IP4 is involved in the interaction and co-localization with RanBPM protein, without being the only interaction site.
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the up-regulated p42(IP4) in Alzheimer's disease neurons may serve as a docking protein to recruit signaling molecules such as different subtypes of casein kinase I to the plasma membrane.
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Results show that nucleolin interacts with centaurin-alpha(1) protein, suggesting that centaurin-alpha(1) may be part of a ribonucleoprotein complex.
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centaurin-alpha1 negatively regulates ARF6 activity by functioning as an in vivo PIP3-dependent ARF6 GAP
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p42IP4 receptor is expressed and distributed throughout the cell in HEK cell lines and is located on chromosome 7, position 7p22.3.
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Authors propose alternative concepts of how elevated levels of p42IP4 might relate to its interaction with nucleolin in the pathomechanisms of Alzheimer's disease.
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The centaurin, alpha 1 protein is a high-affinity PtdIns(3,4,5)P3-binding protein enriched in brain. Sequence analysis indicates centaurin alpha-1 contains two pleckstrin homology domains, ankyrin repeats and an Arf GAP homology domain.
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By acting as a GTPase activating protein for ADP ribosylation factor 6 (ARF6), centaurin alpha 1 is able to switch off ARF6 and inhibit its ability to mediate beta 2-adrenoceptor internalization.
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Centaurin-alpha1 contributes to ERK activation in growth factor signaling, linking the PI3K pathway to the ERK mitogen-activated protein kinase pathway.
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Data show that membrane transport of p42(IP4) induced by epidermal growth factor is inhibited by stimulation of phospholipase C-coupled thrombin receptor.
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p42IP4 binds to nardilysin via the acidic domain, and that this interaction is controlled by the cognate cellular ligands of p42IP4/centaurin-alpha1
