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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

ArfGAP with dual PH domains 1

centaurin-alpha1, p42IP4
binds inositol(1,3,4,5)tetrakisphosphate (InsP4) and phosphatidylinositol(3,4,5)trisphosphate (PtdInsP3);involved in inositol phosphate or inositol lipid signal transduction [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: Alpha-1, ERK1, p16, CAN, Actin
Papers on centaurin-alpha1
Tubulin potentiates the interaction of the metalloendopeptidase nardilysin with the neuronal scaffold protein p42IP4/centaurin-α1 (ADAP1).
Reiser et al., Magdeburg, Germany. In Cell Tissue Res, 2011
Tubulin potentiates the interaction of the metalloendopeptidase nardilysin with the neuronal scaffold protein p42IP4/centaurin-alpha1 (ADAP1).
Phosphorylation-independent dual-site binding of the FHA domain of KIF13 mediates phosphoinositide transport via centaurin alpha1.
Park et al., Toronto, Canada. In Proc Natl Acad Sci U S A, 2010
Full-length KIF13B and CENTA1 form heterotetramers that can bind four phosphoinositide molecules in the vesicle and transport it along the microtubule.
The interaction between casein kinase Ialpha and 14-3-3 is phosphorylation dependent.
Aitken et al., Edinburgh, United Kingdom. In Febs J, 2009
The interaction between CKIalpha and 14-3-3 is dependent on CKIalpha phosphorylation, unlike centaurin-alpha1 (also known as ADAP1), which binds to unphosphorylated CKIalpha on the same region.
The brain-specific protein, p42(IP4) (ADAP 1) is localized in mitochondria and involved in regulation of mitochondrial Ca2+.
Reiser et al., Magdeburg, Germany. In J Neurochem, 2009
In brain, p42(IP4) (centaurin-alpha1; recently named ADAP 1, which signifies ADP ribosylation factor GTPase activating protein with dual PH domains 1, within the large family of Arf-GTPase activating proteins) is mainly expressed in neurons.
Cloning of a centaurin-alpha1 like gene MjCent involved in WSSV infection from shrimp Marsupeneaus japonicus.
Xu et al., Xiamen, China. In Fish Shellfish Immunol, 2009
Centaurin-alpha1 specifically binds phosphatidylinositol 3,4,5-trisphosphate (PI (3,4,5)P3) and is a GTPase-activating protein (GAP) of ADP-ribosylation factor (ARF6).
RanBPM, a novel interaction partner of the brain-specific protein p42IP4/centaurin alpha-1.
Reiser et al., Magdeburg, Germany. In J Neurochem, 2008
The ARFGAP domain of p42IP4 is involved in the interaction and co-localization with RanBPM protein, without being the only interaction site.
The neuronal Arf GAP centaurin alpha1 modulates dendritic differentiation.
Theibert et al., Birmingham, United States. In J Cell Sci, 2007
These data support the conclusion that centaurin alpha1 functions through GAP-dependent Arf regulation of dendritic branching and spines that underlie normal dendritic differentiation and development.
Histochemical evidence for wide expression of the metalloendopeptidase nardilysin in human brain neurons.
Reiser et al., Magdeburg, Germany. In Neuroscience, 2007
Previously, we have detected that nardilysin interacts with brain-specific proteins, i.e. p42(IP4)/centaurin-alpha1 [Stricker R, Chow KM, Walther D, Hanck T, Hersh LB, Reiser G (2006) Interaction of the brain specific protein p42(IP4)/centaurin-alpha1 with the peptidase nardilysin is regulated by the cognate ligands of p42(IP4), PtdIns(3,4,5)P(3) and Ins(1,3,4,5)P(4), with stereospecificity.
Interaction of the brain-specific protein p42IP4/centaurin-alpha1 with the peptidase nardilysin is regulated by the cognate ligands of p42IP4, PtdIns(3,4,5)P3 and Ins(1,3,4,5)P4, with stereospecificity.
Reiser et al., Magdeburg, Germany. In J Neurochem, 2006
p42IP4 binds to nardilysin via the acidic domain, and that this interaction is controlled by the cognate cellular ligands of p42IP4/centaurin-alpha1
Centaurin-alpha1 is a phosphatidylinositol 3-kinase-dependent activator of ERK1/2 mitogen-activated protein kinases.
Nishida et al., Kyoto, Japan. In J Biol Chem, 2006
Centaurin-alpha1 contributes to ERK activation in growth factor signaling, linking the PI3K pathway to the ERK mitogen-activated protein kinase pathway.
Centaurin-alpha1 and KIF13B kinesin motor protein interaction in ARF6 signalling.
Kanamarlapudi, Bristol, United Kingdom. In Biochem Soc Trans, 2005
We have recently isolated a novel KIF (kinesin) motor protein (KIF13B) that binds to centaurin-alpha1, an ARF6GAP that binds to the second messenger PIP3 [PtdIns(3,4,5)P3].
The arf6 GAP centaurin alpha-1 is a neuronal actin-binding protein which also functions via GAP-independent activity to regulate the actin cytoskeleton.
Theibert et al., Birmingham, United States. In Eur J Cell Biol, 2004
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.
Short-term down-regulation of the brain-specific, PtdIns(3,4,5)P3/Ins(1,3,4,5)P4-binding, adapter protein, p42IP4/centaurin-alpha 1 in rat brain after acoustic and electric stimulation.
Yilmazer-Hanke et al., Magdeburg, Germany. In Neurochem Int, 2004
p42IP4, an adapter protein in PIP3-dependent cellular signaling, may play an important role in the signal transduction pathways regulating plasticity in neuronal cells.
Centaurin-alpha1 is an in vivo phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating protein for ARF6 that is involved in actin cytoskeleton organization.
Lawrence et al., Bristol, United Kingdom. In J Biol Chem, 2004
centaurin-alpha1 negatively regulates ARF6 activity by functioning as an in vivo PIP3-dependent ARF6 GAP
Altered expression of protein p42IP4/centaurin-alpha 1 in Alzheimer's disease brains and possible interaction of p42IP4 with nucleolin.
Bernstein et al., Magdeburg, Germany. In Neuroreport, 2004
Authors propose alternative concepts of how elevated levels of p42IP4 might relate to its interaction with nucleolin in the pathomechanisms of Alzheimer's disease.
Identification of gene structure and subcellular localization of human centaurin alpha 2, and p42IP4, a family of two highly homologous, Ins 1,3,4,5-P4-/PtdIns 3,4,5-P3-binding, adapter proteins.
Reiser et al., Magdeburg, Germany. In J Neurochem, 2004
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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