The Role of Phosphatases in Inositol Signaling Reactions

Majerus, PW; Mv, Kisseleva; Fa, Norris

doi:10.1074/jbc.274.16.10669

Cited by 213 publications

(248 citation statements)

References 55 publications

Supporting

Mentioning

233

Contrasting

Unclassified

Order By: Relevance

“…Many different enzymes have been identified that specifically remove phosphate from one or more of the positions on the inositol ring (155,213,240). There is currently evidence for a role in membrane traffic for enzymes that remove phosphate from the D-5 position of PtdIns(4,5)P 2 , the D-5 position of PtdIns(3,5)P 2 , the D-3 position of PtdIns(3,5)P and that remove the phosphate from both PtdIns(4)P and PtdIns(3)P ( Table 2).…”

Section: E Phosphatases Acting On Phosphoinositidesmentioning

confidence: 99%

Phosphoinositides in Constitutive Membrane Traffic

Roth

2004

Physiological Reviews

267

View full text Add to dashboard Cite

Proteins that make, consume, and bind to phosphoinositides are important for constitutive membrane traffic. Different phosphoinositides are concentrated in different parts of the central vacuolar pathway, with phosphatidylinositol 4-phosphate predominate on Golgi, phosphatidylinositol 4,5-bisphosphate predominate at the plasma membrane, phosphatidylinositol 3-phosphate the major phosphoinositide on early endosomes, and phosphatidylinositol 3,5-bisphosphate found on late endocytic organelles. This spatial segregation may be the mechanism by which the direction of membrane traffic is controlled. Phosphoinositides increase the affinity of membranes for peripheral membrane proteins that function for sorting protein cargo or for the docking and fusion of transport vesicles. This implies that constitutive membrane traffic may be regulated by the mechanisms that control the activity of the enzymes that produce and consume phosphoinositides. Although the lipid kinases and phosphatases that function in constitutive membrane traffic are beginning to be identified, their regulation is poorly understood.

show abstract

Section: E Phosphatases Acting On Phosphoinositidesmentioning

confidence: 99%

Phosphoinositides in Constitutive Membrane Traffic

Roth

2004

Physiological Reviews

267

View full text Add to dashboard Cite

show abstract

“…The inositol-polyphosphate 5-phosphatases (referred to as 5-phosphatases) are a large family of signal-modifying enzymes that hydrolyze the 5-phosphate from the inositol ring of both inositol phosphates, such as Ins(1,4,5)P 3 and Ins(1,3,4,5)P 4 , and/or PtdIns-derived messenger molecules, including PtdIns(4,5)P 2 , PtdIns(3,4,5)P 3 , and PtdIns(3,5)P 2 (9). Ten mammalian and four yeast homologs have been identified and characterized.…”

Section: Phosphatidylinositolmentioning

confidence: 99%

Identification of a Novel Domain in Two Mammalian Inositol-polyphosphate 5-Phosphatases That Mediates Membrane Ruffle Localization

Gurung

Tan

Ooms

et al. 2003

Journal of Biological Chemistry

View full text Add to dashboard Cite

SKIP (skeletal muscle and kidney enriched inositol phosphatase) is a recently identified phosphatidylinositol 3,4,5-trisphosphate-and phosphatidylinositol 4,5-bisphosphate-specific 5-phosphatase. In this study, we investigated the intracellular localization of SKIP. Indirect immunofluorescence and subcellular fractionation showed that, in serum-starved cells, both endogenous and recombinant SKIP colocalized with markers of the endoplasmic reticulum (ER). Following epidermal growth factor (EGF) stimulation, SKIP transiently translocated to plasma membrane ruffles and colocalized with submembranous actin. Data base searching demonstrated a novel 128-amino acid domain in the C terminus of SKIP, designated SKICH for SKIP carboxyl homology, which is also found in the 107-kDa 5-phosphatase PIPP and in members of the TRAF6-binding protein family. Recombinant SKIP lacking the SKICH domain localized to the ER, but did not translocate to membrane ruffles following EGF stimulation. The SKIP SKICH domain showed perinuclear localization and mediated EGF-stimulated plasma membrane ruffle localization. The SKICH domain of the 5-phosphatase PIPP also mediated plasma membrane ruffle localization. Mutational analysis identified the core sequence within the SKICH domain that mediated constitutive membrane association and C-terminal sequences unique to SKIP that contributed to ER localization. Collectively, these studies demonstrate a novel membrane-targeting domain that serves to recruit SKIP and PIPP to membrane ruffles.Phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P 2 ) 1 serves as a precursor to two major signaling pathways. This central phosphoinositide is phosphorylated by phosphoinositide 3-kinase, forming PtdIns(3,4,5)P 3 , which transiently accumulates at the plasma membrane of growth factor-activated cells and is subsequently rapidly metabolized by PtdIns(3,4,5)P 3 5-or 3-phosphate-specific lipid phosphatases. PtdIns(3,4,5)P 3 recruits various effector proteins that contain PH domains, such as the serine/threonine kinases Akt and PDK1 (1), and Rho, Rac, and ADP-ribosylation factor guanine nucleotide exchange factors, including P-Rex1 (2) and SWAP-70 (3), which in turn regulate many signaling pathways, including inhibition of cell death, cell cycle progression, actin polymerization, membrane ruffling, cell migration, and secretion (4 -7). In addition, PtdIns(4,5)P 2 is hydrolyzed by phospholipase C to produce inositol 1,4,5-trisphosphate (Ins(1,4,5)P 3 ) and diacylglycerol, which mobilize intracellular calcium and activate protein kinase C, respectively. PtdIns(4,5)P 2 itself regulates the activity of actin-binding proteins by suppressing the function of vinculin, cofilin, gelsolin, and profilin and by activating the actin-gelatinizing activity of ␣-actinin (8).The inositol-polyphosphate 5-phosphatases (referred to as 5-phosphatases) are a large family of signal-modifying enzymes that hydrolyze the 5-phosphate from the inositol ring of both inositol phosphates, such as Ins(1,4,5)P 3 and Ins(1,3,4,5)P 4 , and/or PtdIns-...

show abstract

“…Distinct forms of inositol and phosphatidylinositol 5-phosphatases selectively remove the phosphate from the 5-position of the inositol ring from both soluble and lipid substrates. These enzymes, that terminate the signal transduction processes initiated by PI 3-K, are essential for proper cell function (reviewed in Erneux et al, 1998;Majerus et al, 1999). The Src homology 2 (SH2) domain-containing inositol polyphosphate 5-phosphatase (SHIP) family is a recently described subset of type II 5-phosphatase.…”

mentioning

confidence: 99%

“…The Src homology 2 (SH2) domain-containing inositol polyphosphate 5-phosphatase (SHIP) family is a recently described subset of type II 5-phosphatase. SHIPs are tyrosine-phosphorylated proteins with several interesting features: an amino-terminal SH2 domain, a central catalytic domain and, at the carboxyl tail, several NPxY motifs [able to interact with phosphotyrosine-binding domain (PTB)] and Src homology 3-interacting prolinerich motifs (Drayer et al, 1996;Pesesse et al, 1997;Erneux et al, 1998;Majerus et al, 1999;Rohrschneider et al, 2000). Because of their ability to interact with SH2/PTB-containing protein, such as Src homology 2 domain-containing transforming protein 1 (Shc) (Pradhan and Coggeshall, 1997), and to dephosphorylate phosphatidylinositol 3,4,5-trisphosphate [PtdIns(3,4,5)P 3 ] (Drayer et al, 1996;Pesesse et al, 1998), the SHIPs have the potential to regulate the Ras/MAP kinase pathway and many, if not all, PI 3K induced events.…”

mentioning

confidence: 99%

The SH2 domain-containing 5-phosphatase SHIP2 is expressed in the germinal layers of embryo and adult mouse brain: increased expression in N-CAM-deficient mice

et al. 2001

View full text Add to dashboard Cite

AbstractöThe germinative ventricular zone of embryonic brain contains neural lineage progenitor cells that give rise to neurons, astrocytes and oligodendrocytes. The ability to generate neurons persists at adulthood in restricted brain areas. During development, many growth factors exert their e¡ects by interacting with tyrosine kinase receptors and activate the phosphatidylinositol 3-kinase and the Ras/MAP kinase pathways. By its ability to modulate these pathways, the recently identi¢ed Src homology 2 domain-containing inositol polyphosphate 5-phosphatase 2, SHIP2, has the potential to regulate neuronal development. Using in situ hybridization technique with multiple synthetic oligonucleotides, we demonstrated that SHIP2 mRNA was highly expressed in the ventricular zone at early embryonic stages and subventricular zones at latter stages of brain and spinal cord and in the sympathetic chain. No signi¢cant expression was seen in di¡erentiated ¢elds. This restricted expression was maintained from embryonic day 11.5 to birth. In the periphery, large expression was detected in muscle and kidney and moderate expression in thyroid, pituitary gland, digestive system and bone. In the adult brain, SHIP2 was mainly restricted in structures containing neural stem cells such as the anterior subventricular zone, the rostral migratory stream and the olfactory tubercle. SHIP2 was also detected in the choroid plexuses and the granular layer of the cerebellum. The speci¢city of SHIP2 expression in neural stem cells was further demonstrated by (i) the dramatic increase in SHIP2 mRNA signal in neural cell adhesion molecule (N-CAM)-de¢cient mice, which present an accumulation of progenitor cells in the anterior subventricular zone and the rostral migratory stream, (ii) the abundant expression of 160-kDa SHIP2 by western blotting in proliferating neurospheres in culture and its downregulation in non-proliferating di¡erentiated neurospheres.In conclusion, the close correlation between the pattern of SHIP2 expression in the brain and the proliferative and early di¡erentiative events suggests that the phosphatase SHIP2 may have important roles in neural development. ß

show abstract

The Role of Phosphatases in Inositol Signaling Reactions

Cited by 213 publications

References 55 publications

Phosphoinositides in Constitutive Membrane Traffic

Phosphoinositides in Constitutive Membrane Traffic

Identification of a Novel Domain in Two Mammalian Inositol-polyphosphate 5-Phosphatases That Mediates Membrane Ruffle Localization

The SH2 domain-containing 5-phosphatase SHIP2 is expressed in the germinal layers of embryo and adult mouse brain: increased expression in N-CAM-deficient mice

Contact Info

Product

Resources

About