Expression and Subcellular Localization of p42<sup>IP4</sup>/ Centaurin‐α, a Brain‐specific, High‐affinity Receptor for lnositol 1,3,4,5‐Tetrakisphosphate and Phosphatidylinositol 3,4,5‐Trisphosphate in Rat Brain

Kreutz, Michael R.; Böckers, Tobias M.; Sabel, Bernhard A.; Hülser, E; Stricker, Rolf; Reiser, Georg

doi:10.1111/j.1460-9568.1997.tb01378.x

Cited by 39 publications

(29 citation statements)

References 43 publications

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“…Centaurin ␣1 expressed in the adult is also associated with the synaptosome fraction. This result is in agreement with immunohistochemistry results that show centaurin-␣1/p42IP4 localizes to synaptic regions in neuronal sections (Kreutz et al, 1997;Sedehizade et al, 2002) and is consistent with the identification of centaurin ␣1 in the post-synaptic density fraction by proteomic analysis (Yoshimura et al, 2004).…”

Section: Developmental Expression and Localization Of Endogenous Centsupporting

confidence: 80%

The neuronal Arf GAP centaurin α1 modulates dendritic differentiation

Moore

Thacker

Larimore

et al. 2007

Journal of Cell Science

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ReferencesAggensteiner, M. and Reiser, G. (2003). Expression of the brain-specific membrane adapter protein p42 IP4 /centaurin a, a Ins(1,3,4,5)P 4 /PtdIns(3,4,5)P 3 binding protein, in developing rat brain. Brain Res. Dev. Brain Res. 142,[77][78][79][80][81][82][83][84][85][86][87]. Albertinazzi, C., Za, L., Paris, S. and de Curtis, I. (2003). ADP-ribosylation factor 6 and a functional PIX/p95-APP1 complex are required for Rac1B-mediated neurite outgrowth. Mol. Biol. Cell 14, 1295-1307. Allen, P., Ouimet, C. and Greengard, P. (1997 (1996). Identification and cloning of centaurin alpha: a novel phosphatidylinositol (3,4,5)-trisphosphate binding protein from rat brain.

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Section: Developmental Expression and Localization Of Endogenous Centsupporting

confidence: 80%

The neuronal Arf GAP centaurin α1 modulates dendritic differentiation

Moore

Thacker

Larimore

et al. 2007

Journal of Cell Science

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“…1B). Recognition by this antiserum confirms unequivocally the identity of the recombinant protein as we have demonstrated previously that the antiserum stains p42 IP4 specifically in Western blots [31] and also in immunohistochemistry of brain sections [35]. The recombinant GST±p42 IP4 fusion protein was also detectable by a rabbit polyclonal anti-GST antiserum (Fig.…”

Section: Q Febs 1999supporting

confidence: 49%

Recombinant p42^IP4, a brain‐specific 42‐kDa high‐affinity Ins(1,3,4,5)P₄ receptor protein, specifically interacts with lipid membranes containing Ptd‐Ins(3,4,5)P₃

Hanck

Stricker

Krishna

et al. 1999

European Journal of Biochemistry

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We have recently cloned the cDNA of p42 IP4 , a membrane-associated and cytosolic inositol (1,3,4,5)tetrakisphosphate receptor protein [Stricker, R., Hu Èlser, E., Fischer, J., Jarchau, T., Walter, U., Lottspeich, F. & Reiser, G. (1997) FEBS Lett. 405, 229±236.] p42 IP4 is a protein of 374 amino acids with M r of 42 kDa. The p42 IP4 protein has a zinc finger motif at its N-terminus, followed by two pleckstrin homology domains. To characterize further the biochemical and functional properties of p42 IP4 , it was expressed as a glutathione-S-transferase fusion protein in Sf9 cells using a recombinant baculovirus vector. The protein was affinity adsorbed on glutathione beads, cleaved from glutathione-S-transferase with the protease factor-Xa and purified on heparin agarose. The recombinant purified protein is active because it shows binding affinities similar to those of the native p42 IP4 , purified from pig cerebellum or rat brain (K i for inositol(1,3,4,5)P 4 of 4.1 nm and 2.2 nm, respectively). Moreover the ligand specificity of the recombinant protein for various inositol polyphosphates is similar to that of the native protein purified from brain. Importantly, we show here that p42 IP4 binds phosphatidylinositol(3,4,5)P 3 specifically, as the recombinant protein can associate with lipid membranes (vesicles) containing phosphatidylinositol(3,4,5)P 3 ; this binding occurs in a concentration-dependent manner and is blocked by inositol(1,3,4,5)P 4 . This specific association and the possibility that endogenous p42 IP4 can be converted from a membrane-associated state to a soluble state support the hypothesis that p42 IP4 might be redistributed between cellular compartments upon hormonal stimulation.Keywords: baculovirus; inositolP 4 ; membrane interaction; pleckstrin homology domain; phosphatidylinositolP 3 ; receptor; vesicle association.Two second messengers, inositol 1,4,5-trisphosphate [Ins(1,4,5)P 3 ] and diacylglycerol, are produced from phosphatidylinositol 4,5-bisphosphate [Ptd-Ins(4,5)P 2 ]. The generation of Ptd-Ins(4,5)P 2 and its cleavage by phospholipase C (PLC) are tightly regulated signal transduction pathways [1]. Ins(1,4,5)P 3 mobilizes Ca 2+ from intracellular stores whereas diacylglycerol activates protein kinase C [2]. During the last few years, the putative second messengers Ins(1,3,4,5)P 4 and Ptd-Ins(3,4,5)P 3 , which are generated by phosphorylating the D3 position of the inositol ring, have attracted increasing interest. The functions of Ins(1,3,4,5)P 4 and Ptd-Ins(3,4,5)P 3 are much less clear than that of Ins(1,4,5)P 3 [2]. Ptd-Ins(3,4,5)P 3 is the product of class I phosphoinositide kinases. Phosphoinositide-3-kinase (PI3-kinase) a is regulated by membrane-bound receptor tyrosine kinases [3] whereas PI3-kinase g is activated by heterotrimeric G-proteins [4]. Ins(1,4,5)P 3 can be phosphorylated to Ins(1,3,4,5)P 4 by Ins(1,4,5)P 3 -3-kinase [5].The physiological role of Ins(1,3,4,5)P 4 is still widely disputed [6]. Ptd-Ins(3,4,5)P 3 has been demonstrated to be an important regulator of me...

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“…Moreover, CKI␣ has been found to co-localize in neurones with synaptic vesicle markers and phosphorylates some vesicle synaptic associated proteins (21). Interestingly, centaurin-␣ 1 has been shown to associate with presynaptic vesicular structures (53). An actin-associated protein kinase shown to be a member of the CKI family phosphorylates actin in vitro (54).…”

Section: Discussionmentioning

confidence: 99%

Casein Kinase I Associates with Members of the Centaurin-α Family of Phosphatidylinositol 3,4,5-Trisphosphate-binding Proteins

Dubois

Kerai

Zemlickova

et al. 2001

Journal of Biological Chemistry

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Mammalian casein kinases I (CKI) belong to a family of serine/threonine protein kinases involved in diverse cellular processes including cell cycle progression, membrane trafficking, circadian rhythms, and Wnt signaling. Here we show that CKI␣ co-purifies with centaurin-␣ 1 in brain and that they interact in vitro and form a complex in cells. In addition, we show that the association is direct and occurs through the kinase domain of CKI within a loop comprising residues 217-233. These residues are well conserved in all members of the CKI family, and we show that centaurin-␣ 1 associates in vitro with all mammalian CKI isoforms. To date, CKI␣ represents the first protein partner identified for centaurin-␣ 1 . However, our data suggest that centaurin-␣ 1 is not a substrate for CKI␣ and has no effect on CKI␣ activity. Centaurin-␣ 1 has been identified as a phosphatidylinositol 3,4,5-trisphosphate-binding protein. Centaurin-␣ 1 contains a cysteine-rich domain that is shared by members of a newly identified family of ADPribosylation factor guanosine trisphosphatase-activating proteins. These proteins are involved in membrane trafficking and actin cytoskeleton rearrangement, thus supporting a role for CKI␣ in these biological events.

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Expression and Subcellular Localization of p42^IP4/ Centaurin‐α, a Brain‐specific, High‐affinity Receptor for lnositol 1,3,4,5‐Tetrakisphosphate and Phosphatidylinositol 3,4,5‐Trisphosphate in Rat Brain

Cited by 39 publications

References 43 publications

The neuronal Arf GAP centaurin α1 modulates dendritic differentiation

The neuronal Arf GAP centaurin α1 modulates dendritic differentiation

Recombinant p42^IP4, a brain‐specific 42‐kDa high‐affinity Ins(1,3,4,5)P₄ receptor protein, specifically interacts with lipid membranes containing Ptd‐Ins(3,4,5)P₃

Casein Kinase I Associates with Members of the Centaurin-α Family of Phosphatidylinositol 3,4,5-Trisphosphate-binding Proteins

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Expression and Subcellular Localization of p42IP4/ Centaurin‐α, a Brain‐specific, High‐affinity Receptor for lnositol 1,3,4,5‐Tetrakisphosphate and Phosphatidylinositol 3,4,5‐Trisphosphate in Rat Brain

Cited by 39 publications

References 43 publications

The neuronal Arf GAP centaurin α1 modulates dendritic differentiation

The neuronal Arf GAP centaurin α1 modulates dendritic differentiation

Recombinant p42IP4, a brain‐specific 42‐kDa high‐affinity Ins(1,3,4,5)P4 receptor protein, specifically interacts with lipid membranes containing Ptd‐Ins(3,4,5)P3

Casein Kinase I Associates with Members of the Centaurin-α Family of Phosphatidylinositol 3,4,5-Trisphosphate-binding Proteins

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Expression and Subcellular Localization of p42^IP4/ Centaurin‐α, a Brain‐specific, High‐affinity Receptor for lnositol 1,3,4,5‐Tetrakisphosphate and Phosphatidylinositol 3,4,5‐Trisphosphate in Rat Brain

Recombinant p42^IP4, a brain‐specific 42‐kDa high‐affinity Ins(1,3,4,5)P₄ receptor protein, specifically interacts with lipid membranes containing Ptd‐Ins(3,4,5)P₃