Regulation of PLC-mediated signalling in vivo by CDP-diacylglycerol synthase

Wu, Louisa P.; Niemeyer, Barbara A.; Colley, Nansi Jo; Socolich, Michael; Zuker, Charles S.

doi:10.1038/373216a0

Cited by 166 publications

(160 citation statements)

References 48 publications

Supporting

Mentioning

156

Contrasting

Order By: Relevance

“…These include the DAG kinase (RDGA), cytidine diphosphate (CDP)-DAG synthase (CDS) and the PI synthase (PIS), which catalyzes the production of phosphatidic acid (PA), CDP-DAG, and PI, respectively (Fig. 6a) [28,29,[131][132][133]. In addition, a PI transfer protein (RDGB) may function in the transfer of PIs from the SRC to the rhabdomeres [29,134,135].…”

Section: G Q Protein In Phototransductionmentioning

confidence: 99%

“…In addition, a PI transfer protein (RDGB) may function in the transfer of PIs from the SRC to the rhabdomeres [29,134,135]. If the levels of CDS or PIS are reduced but not eliminated, a light response can still be obtained if the flies are dark-adapting [131,132]. However, the flies are not able to sustain a light response.…”

Section: G Q Protein In Phototransductionmentioning

confidence: 99%

“…Light-dependent retinal degeneration results from disruption of other proteins that function in the PIP 2 regeneration cycle, including RDGB (PI transfer protein), CDS (CDP-DAG synthase), and dPIS (PI synthase) [28,29,131,132,229]. Overexpression of PLD, which might lead to the generation of higher levels of PIP 2 through conversion of PC to PA, suppresses the retinal degeneration in the rdgB mutant [137].…”

Section: Disruption Of Pi Cycle Leads To Retinal Degenerationmentioning

confidence: 99%

See 2 more Smart Citations

Phototransduction and retinal degeneration in Drosophila

Wang

Montell

2007

Pflugers Arch - Eur J Physiol

261

303

View full text Add to dashboard Cite

Drosophila visual transduction is the fastest known G-protein-coupled signaling cascade and has therefore served as a genetically tractable animal model for characterizing rapid responses to sensory stimulation. Mutations in over 30 genes have been identified, which affect activation, adaptation, or termination of the photoresponse. Based on analyses of these genes, a model for phototransduction has emerged, which involves phosphoinoside signaling and culminates with opening of the TRP and TRPL cation channels. Many of the proteins that function in phototransduction are coupled to the PDZ containing scaffold protein INAD and form a supramolecular signaling complex, the signalplex. Arrestin, TRPL, and Gα q undergo dynamic light-dependent trafficking, and these movements function in long-term adaptation. Other proteins play important roles either in the formation or maturation of rhodopsin, or in regeneration of phosphatidylinositol 4,5-bisphosphate (PIP 2 ), which is required for the photoresponse. Mutation of nearly any gene that functions in the photoresponse results in retinal degeneration. The underlying bases of photoreceptor cell death are diverse and involve mechanisms such as excessive endocytosis of rhodopsin due to stable rhodopsin/arrestin complexes and abnormally low or high levels of Ca 2+ . Drosophila visual transduction appears to have particular relevance to the cascade in the intrinsically photosensitive retinal ganglion cells in mammals, as the photoresponse in these latter cells appears to operate through a remarkably similar mechanism.

show abstract

Section: G Q Protein In Phototransductionmentioning

confidence: 99%

Section: G Q Protein In Phototransductionmentioning

confidence: 99%

Section: Disruption Of Pi Cycle Leads To Retinal Degenerationmentioning

confidence: 99%

See 1 more Smart Citation

Phototransduction and retinal degeneration in Drosophila

Wang

Montell

2007

Pflugers Arch - Eur J Physiol

261

303

View full text Add to dashboard Cite

show abstract

“…Recent immunolocalization studies by Lee et al (2003) have shown that light-dependant translocation of Arr2 to and from the rhabdomere is impaired in cds (Wu et al, 1995) and rdgB (Vihtelic et al, 1993(Vihtelic et al, ,1991 mutants, in which PI biogenesis and trafficking are disrupted, respectively. They, furthermore, showed that in PTEN; dAkt and PTEN overexpression (Huang et al, 1999;Stocker et al, 2002) mutants, in which metabolism of PIP 3 is defective, Arr2 translocation was also impaired.…”

Section: Light Adaptation Through Phosphoinositide and Ninac Myosin Imentioning

confidence: 99%

Light-regulated translocation of signaling proteins in Drosophila photoreceptors

Frechter

Minke

2006

Journal of Physiology-Paris

View full text Add to dashboard Cite

Illumination of Drosophila photoreceptor cells induces multi-facet responses, which include generation of the photoreceptor potential, screening pigment migration and translocation of signaling proteins which is the focus of recent extensive research. Translocation of three signaling molecules is covered in this review: (1) Light-dependent translocation of arrestin from the cytosol to the signaling membrane, the rhabdomere, determines the lifetime of activated rhodopsin. Arrestin translocates in PIP 3 and NINAC myosin III dependent manner, and specific mutations which disrupt the interaction between arrestin and PIP 3 or NINAC also impair the light-dependant translocation of arrestin and the termination of the response to light. (2) Activation of Drosophila visual G protein, DGq, causes a massive and reversible, translocation of the α subunit from the signaling membrane to the cytosol, accompanied by activity-dependent architectural changes. Analysis of the translocation and the recovery kinetics of DGq α in wild-type flies and specific visual mutants indicated that DGq α is necessary but not sufficient for the architectural changes. (3) The TRP-like (TRPL) but not TRP channels translocate in a light-dependent manner between the rhabdomere and the cell body. As a physiological consequence of this light-dependent modulation of the TRP/TRPL ratio, the photoreceptors of dark-adapted flies operate at a wider dynamic range, which allows the photoreceptors enriched with TRPL to function better in darkness and dim background illumination. Altogether, signal-dependent movement of signaling proteins plays a major role in the maintenance and function of photoreceptor cells.

show abstract

“…Two overlapping ESTs from Arabidopsis tkaliana, T45653 and N97146, were found with a "bait" amino acid sequence of CDS from Esckerickia coli. The ESTs contained a continuous open reading frame that encoded a partia1 protein with highest sequence homology to the CDS of Drosophila melanogaster (Wu et al, 1995) and Sacchnromyces cerevisiae (Shen et al, 1996). A 317-bp molecular probe was generated by PCR with forward primer 5'-GGCCTTTAATAAAGCTGTCTCC-3' and reverse primer 5'-TACCGAAAAACCCCCCAAAAGG-3' from 50 ng of first-strand cDNA, which was prepared from poly(A)+ RNA of rosette leaves of A. tkaliana ecotype C-24.…”

Section: Cloning and Sequencing Of Cdnasmentioning

confidence: 99%

Complementary DNAs Encoding Eukaryotic-Type Cytidine-5[prime]-Diphosphate-Diacylglycerol Synthases of Two Plant Species

1997

View full text Add to dashboard Cite

Cytidine diphosphate (CDP)-diacylglycerol synthase (cytidine triph0sphate:phosphatidate cytidyltransferase, EC 2.7.7.41) catalyzes the formation of CDP-diacylglycerol, which is the precursor of phosphatidylinositol, phosphatidylglycerol, and cardiolipin. We report the first cloning, to our knowledge, of two plant cDNAs, StCDSl and AtCDS1, coding for CDP-diacylglycerol synthases from potato (Solanum tuberosum) and Arabidopsis thaliana, respectively. The two proteins belong to the eukaryotic type of CDP-diacylglycerol synthases and contain eight predicted transmembrane-spanning domains. We analyzed gene expression in shoot and root tissues of potato plants and demonstrated enzyme activity by expression of N-terminally truncated, recombinant StCDSl in Escherichia coli.CDS (cytidine triph0sphate:phosphatidate cytidyltransferase, EC 2.7.7.41) catalyzes the synthesis of CDP-DG and PPi from PA and CTP. CDP-DG is the precursor of the minor lipids PI, PG (via PG phosphate), cardiolipin, and possibly phosphatidylserine (Moore, 1982). CDS activity is present in most plant membrane systems. Located at the inner envelope membrane of chloroplasts, CDS may be mainly engaged in PG synthesis (Andrews and Mudd, 1985). In mitochondria, CDP-DG is the substrate for PG phosphate synthase (EC 2.7.8.5) and cardiolipin synthase. CDS and other enzymes involved in cardiolipin biosynthesis are enriched at the inner mitochondrial membrane (Frentzen and Griebau, 1994). Microsomes isolated from castor bean endosperm contain approximately 75% of total extractable CDS activity (Kleppinger-Sparace and Moore, 1985). Microsomal membranes might account for most of the PI synthesis in plant cells (Moore, 1982). Studies on microsomes isolated from spinach leaves also suggest the presence of phosphatidylserine synthase (EC 2.7.8.8), which utilizes CDP-DG (Marshall and Kates, 1974). Moreover, CDS and other enzymes necessary for PI resynthesis from phospholipase C and D reaction products are present in plant plasma membranes (Wissing et al., 1992). As demonstrated by the recent discovery of an eye-specific CDS from Drosophila melanogaster, CDS activity is essential for IP,-mediated light perception in insect eyes (Wu et al., To investigate the role of CDS in plants we isolated and characterized the first plant cDNA clones of this enzyme. We present the predicted primary structures and properties of CDS from potato (Solanum tuberosum) (StCDSl) and Arabidopsis tkaliana (AtCDSl), a preliminary analysis of gene expression in potato plants, and enzyme activity of recombinant StCDSl. MATERIALS A N D METHODS Cloning and Sequencing of cDNAsA TBLASTN search (Altschul et al., 1990) for CDS homologous plant sequences was performed in the EST database at the National Center of Biotechnology Information (Bethesda, MD). Two overlapping ESTs from Arabidopsis tkaliana, T45653 and N97146, were found with a "bait" amino acid sequence of CDS from Esckerickia coli. The ESTs contained a continuous open reading frame that encoded a partia1 protein with highest sequence homol...

show abstract

Regulation of PLC-mediated signalling in vivo by CDP-diacylglycerol synthase

Cited by 166 publications

References 48 publications

Phototransduction and retinal degeneration in Drosophila

Phototransduction and retinal degeneration in Drosophila

Light-regulated translocation of signaling proteins in Drosophila photoreceptors

Complementary DNAs Encoding Eukaryotic-Type Cytidine-5[prime]-Diphosphate-Diacylglycerol Synthases of Two Plant Species

Contact Info

Product

Resources

About