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

Inositol polyphosphate-5-phosphatase, 75kDa

Inpp5b, phosphoinositide 5-phosphatase, 75-kDa inositol polyphosphate-5-phosphatase, 5-ptase
Cellular calcium signaling is controlled by the production of inositol phosphates (IPs) by phospholipase C in response to extracellular signals. The IP signaling molecules are inactivated by a family of inositol polyphosphate-5-phosphatases (5-phosphatases). This gene encodes the type II 5-phosphatase. The protein is localized to the cytosol and mitochondria, and associates with membranes through an isoprenyl modification near the C-terminus. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Actin, SHIP2, ACID, V1a, IB1
Papers using Inpp5b antibodies
An Arabidopsis purple acid phosphatase with phytase activity increases foliar ascorbate
Khodakovskaya Mariya V. et al., In Journal of Experimental Botany, 2007
... InsP 5-ptase transgenic plants ...
Papers on Inpp5b
Phosphoinositides Regulate Ciliary Protein Trafficking to Modulate Hedgehog Signaling.
Reiter et al., San Francisco, United States. In Dev Cell, Sep 2015
This distribution is created by Inpp5e, a ciliary phosphoinositide 5-phosphatase.
Reversible chemical dimerizer-induced recovery of PIP2 levels moves clathrin to the plasma membrane.
Schultz et al., Heidelberg, Germany. In Bioorg Med Chem, Jul 2015
Here we have applied this system to transiently activate phosphatidylinositol 4,5-bisphosphate (PIP2) breakdown at the PM via translocation of phosphoinositide 5-phosphatase (5Ptase).
Primary root protophloem differentiation requires balanced phosphatidylinositol-4,5-biphosphate levels and systemically affects root branching.
Hardtke et al., Lausanne, Switzerland. In Development, May 2015
Second site mutation in the protophloem-specific presumed phosphoinositide 5-phosphatase cotyledon vascular pattern 2 (CVP2), but not in its homolog CVP2-like 1 (CVL1), partially rescues brx defects.
OCRL-mutated fibroblasts from patients with Dent-2 disease exhibit INPP5B-independent phenotypic variability relatively to Lowe syndrome cells.
Dorseuil et al., Paris, France. In Hum Mol Genet, Mar 2015
Finally, we analyzed INPP5B, a paralogous gene already reported to exhibit functional redundancy with OCRL, and report neither differences in its expression at RNA or protein levels, nor specific allelic variations between fibroblasts of patients.
Identification of inhibitors of inositol 5-phosphatases through multiple screening strategies.
De Camilli et al., New Haven, United States. In Acs Chem Biol, 2014
Two prominent chemical scaffolds were identified with high nanomolar/low micromolar activity, with one class showing inhibitory activity toward all 5-phosphatases tested and the other selective activity toward OCRL and INPP5B, which are closely related to each other.
Structural basis for phosphoinositide substrate recognition, catalysis, and membrane interactions in human inositol polyphosphate 5-phosphatases.
Nordlund et al., Stockholm, Sweden. In Structure, 2014
SHIP2, OCRL, and INPP5B belong to inositol polyphosphate 5-phophatase subfamilies involved in insulin regulation and Lowes syndrome.
Comparative genomics of pneumocystis species suggests the absence of genes for myo-inositol synthesis and reliance on inositol transport and metabolism.
Cushion et al., Cincinnati, United States. In Mbio, 2013
phosphoinositide 5-phosphatase (EC, and inositol-1,4-bisphosphate 1-phosphatase (EC, were identified in the two rodent Pneumocystis genomes, P. carinii and P. murina.
Mechanistic insights into the regulation of circular dorsal ruffle formation.
Hasegawa et al., Kōbe, Japan. In J Biochem, 2013
Among them, the roles of PI3-kinase and phosphoinositide 5-phosphatase may hold the key to the induction of these circular structures.
Compensatory Role of Inositol 5-Phosphatase INPP5B to OCRL in Primary Cilia Formation in Oculocerebrorenal Syndrome of Lowe.
Sun et al., Indianapolis, United States. In Plos One, 2012
INPP5B is a paralog of OCRL and shares similar structural domains.
Developmental defects and rescue from glucose intolerance of a catalytically-inactive novel Ship2 mutant mouse.
Schurmans et al., Brussels, Belgium. In Cell Signal, 2012
The function of the phosphoinositide 5-phosphatase Ship2 was investigated in a new mouse model expressing a germline catalytically-inactive Ship2(∆/∆) mutant protein.
OCRL localizes to the primary cilium: a new role for cilia in Lowe syndrome.
Sun et al., Indianapolis, United States. In Hum Mol Genet, 2012
OCRL is a phosphoinositide 5-phosphatase that interacts with small GTPases and is involved in intracellular trafficking.
Impaired neural development in a zebrafish model for Lowe syndrome.
Lowe et al., Manchester, United Kingdom. In Hum Mol Genet, 2012
Lowe syndrome, which is characterized by defects in the central nervous system, eyes and kidneys, is caused by mutation of the phosphoinositide 5-phosphatase OCRL1.
Yersinia entry into host cells requires Rab5-dependent dephosphorylation of PI(4,5)P₂ and membrane scission.
Grinstein et al., Toronto, Canada. In Cell Host Microbe, 2012
At the time of scission, the inositol 5-phosphatases OCRL and Inpp5b were recruited to prevacuoles.
The host phosphoinositide 5-phosphatase SHIP2 regulates dissemination of vaccinia virus.
Kalman et al., Atlanta, United States. In J Virol, 2011
We found that the phosphoinositide 5-phosphatase SHIP2 localizes to actin tails.
Species-specific difference in expression and splice-site choice in Inpp5b, an inositol polyphosphate 5-phosphatase paralogous to the enzyme deficient in Lowe Syndrome.
Nussbaum et al., San Francisco, United States. In Mamm Genome, 2010
study found mouse Inpp5b and human INPP5B differ in their transcription, splicing and amino acid sequence; observations form foundation for analyzing the functional basis for the difference in how Inpp5b and INPP5B compensate for loss of Ocrl function
Lowe syndrome patient fibroblasts display Ocrl1-specific cell migration defects that cannot be rescued by the homologous Inpp5b phosphatase.
Aguilar et al., West Lafayette, United States. In Hum Mol Genet, 2010
The homologous phosphatase Inpp5b was unable to complement the Ocrl1-dependent cell migration defect.
A PH domain within OCRL bridges clathrin-mediated membrane trafficking to phosphoinositide metabolism.
De Camilli et al., New Haven, United States. In Embo J, 2009
The NH2-terminal region of OCRL, but not of INPP5B, binds clathrin heavy chain.
Targeting of the type II inositol polyphosphate 5-phosphatase INPP5B to the early secretory pathway.
Lowe et al., Manchester, United Kingdom. In J Cell Sci, 2007
INPP5B is also localised to the early secretory pathway including the Golgi apparatus and ER-to-Golgi intermediate compartment (ERGIC).
Sac phosphatase domain proteins.
Parker et al., London, United Kingdom. In Biochem J, 2000
The Sac phosphatase domain is also found within the mammalian phosphoinositide 5-phosphatase synaptojanin and the yeast synaptojanin homologues Inp51p, Inp52p and Inp53p.
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