NUCB1, the Drosophila melanogaster homolog of the mammalian EF-hand proteins NEFA and nucleobindin

Otte, Stefan; Barnikol-Watanabe, Shitsu; Vorbrüggen, Gerd; Hilschmann, Norbert

doi:10.1016/s0925-4773(99)00103-3

Cited by 20 publications

(17 citation statements)

References 13 publications

(12 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…NUCB1 is associated with the Golgi apparatus, but its exact role remains unknown in Drosophila. 45 In agreement with its RSA specific interaction, it was shown that Drosophila generates the mucin-type T-antigen (Gal 1-3GalNAcR-Ser/Thr) as predominant O-glycan structure on glycoproteins. 21 Mutations in one member of the enzymes responsible for mucin-type O-glycosylation (pgant35A) was even shown to abrogate enzymatic activity with death occurring throughout development, 19 illustrating the crucial role for this type of O-glycans during development of Drosophila.…”

Section: Research Articlesmentioning

confidence: 86%

Glycosylation Signatures in Drosophila: Fishing with Lectins

et al. 2010

View full text Add to dashboard Cite

Glycosylation is a co- and/or post-translational protein modification that generates enormous structural diversity among glycoproteins. In this study, immobilized lectins were used to capture glycoproteins with different glycan profiles from Drosophila melanogaster extracts. On the basis of previous results from glycan array analyses, the snowdrop (Galanthus nivalis) agglutinin (GNA), the tobacco (Nicotiana tabacum) lectin (Nictaba) and the Rhizoctoni solani agglutinin (RSA) were used to select for a broad range of N- and O-glycan structures. After different lectin affinity chromatographies, the glycoproteome of Drosophila was analyzed using LC-MS/MS and glycoprotein abundances were calculated by different label-free methods. Bioinformatics tools were used to annotate the identified glycoproteins and the glycoproteins were classified according to their molecular function or their involvement in a biological process. Subsequent enrichment analysis (using the DAVID database) was employed to find biological processes or molecular functions in Drosophila in which a particular glycan signature is overrepresented. The results presented here clearly demonstrate that next to the presence of high-mannose and pauci-mannose N-glycans, Drosophila is capable of synthesizing glycoproteins carrying extended hybrid and complex N-linked glycans. Furthermore, it was demonstrated that a specific glycosylation signature can be associated with a functionally related group of glycoproteins in Drosophila, both in terms of biological process and molecular function.

show abstract

Section: Research Articlesmentioning

confidence: 86%

Glycosylation Signatures in Drosophila: Fishing with Lectins

et al. 2010

View full text Add to dashboard Cite

show abstract

“…NucB1, a Golgi apparatus resident protein, has been localized specifically to salivary tissues in Drosophila melanogaster by in situ hybridization (52), and the enzyme activity of FE4-esterase was found in the saliva of Aedes aegypti (2). A number of different cuticle proteins were predicted to function at the gut (Table 4).…”

Section: Discussionmentioning

confidence: 99%

Genetics Coupled to Quantitative Intact Proteomics Links Heritable Aphid and Endosymbiont Protein Expression to Circulative Polerovirus Transmission

Cilia

Tamborindeguy

Fish

et al. 2011

J Virol

108

View full text Add to dashboard Cite

Yellow dwarf viruses in the family Luteoviridae, which are the causal agents of yellow dwarf disease in cereal crops, are each transmitted most efficiently by different species of aphids in a circulative manner that requires the virus to interact with a multitude of aphid proteins. Aphid proteins differentially expressed in F2 Schizaphis graminum genotypes segregating for the ability to transmit Cereal yellow dwarf virus-RPV (CYDV-RPV) were identified using two-dimensional difference gel electrophoresis (DIGE) coupled to either matrix-assisted laser desorption ionization-tandem mass spectrometry or online nanoscale liquid chromatography coupled to electrospray tandem mass spectrometry. A total of 50 protein spots, containing aphid proteins and proteins from the aphid's obligate and maternally inherited bacterial endosymbiont, Buchnera, were identified as differentially expressed between transmission-competent and refractive aphids. Surprisingly, in virus transmission-competent F2 genotypes, the isoelectric points of the Buchnera proteins did not match those in the maternal Buchnera proteome as expected, but instead they aligned with the Buchnera proteome of the transmission-competent paternal parent. Among the aphid proteins identified, many were involved in energy metabolism, membrane trafficking, lipid signaling, and the cytoskeleton. At least eight aphid proteins were expressed as heritable, isoelectric point isoform pairs, one derived from each parental lineage. In the F2 genotypes, the expression of aphid protein isoforms derived from the competent parental lineage aligned with the virus transmission phenotype with high precision. Thus, these isoforms are candidate biomarkers for CYDV-RPV transmission in S. graminum. Our combined genetic and DIGE approach also made it possible to predict where several of the proteins may be expressed in refractive aphids with different barriers to transmission. Twelve proteins were predicted to act in the hindgut of the aphid, while six proteins were predicted to be associated with the accessory salivary glands or hemolymph. Knowledge of the proteins that regulate virus transmission and their predicted locations will aid in understanding the biochemical mechanisms regulating circulative virus transmission in aphids, as well as in identifying new targets to block transmission.

show abstract

“…4C). Invertebrate homologs of mammalian Nuc and NEFA isolated from insects Spodoptera frugiperda and Drosophila melanogaster possess two EF-hand motifs and intervening acidic region but no Leu zipper (25,26), indicating that the Ca 2ϩ -binding domain is evolutionally conserved. Because necdin binds to the region encompassing the two EF hand motifs ( Fig.…”

Section: Discussionmentioning

confidence: 99%

The Postmitotic Growth Suppressor Necdin Interacts with a Calcium-binding Protein (NEFA) in Neuronal Cytoplasm

Taniguchi¹,

Taniura²,

Niinobe³

et al. 2000

Journal of Biological Chemistry

View full text Add to dashboard Cite

Necdin, a growth suppressor expressed predominantly in postmitotic neurons, interacts with viral oncoproteins and cellular transcription factors E2F1 and p53. In search of other cellular targets of necdin, we screened cDNA libraries from neurally differentiated murine embryonal carcinoma P19 cells and adult rat brain by the yeast two-hybrid assay. We isolated cDNAs encoding partial sequences of mouse NEFA and rat nucleobindin (CALNUC), which are Ca 2؉ -binding proteins possessing similar domain structures. Necdin interacted with NEFA via a domain encompassing two EF hand motifs, which had Ca 2؉ binding activity as determined by 45 Ca 2؉ overlay. NEFA was widely distributed in mouse organs, whereas necdin was expressed predominantly in the brain and skeletal muscle. In mouse brain in vivo, NEFA was localized in neuronal perikarya and dendrites. By immunoelectron microscopy, NEFA was localized to the cisternae of the endoplasmic reticulum and nuclear envelope in brain neurons. NEFAgreen fluorescent protein (GFP) fusion protein expressed in neuroblastoma N1E-115 cells was retained in the cytoplasm and partly secreted into the culture medium. Necdin enhanced the cytoplasmic retention of NEFA-GFP and potentiated the effect of NEFA-GFP on caffeine-evoked elevation of cytosolic Ca 2؉ levels. Thus, necdin and NEFA might be involved in Ca 2؉ homeostasis in neuronal cytoplasm.

show abstract

NUCB1, the Drosophila melanogaster homolog of the mammalian EF-hand proteins NEFA and nucleobindin

Cited by 20 publications

References 13 publications

Glycosylation Signatures in Drosophila: Fishing with Lectins

Glycosylation Signatures in Drosophila: Fishing with Lectins

Genetics Coupled to Quantitative Intact Proteomics Links Heritable Aphid and Endosymbiont Protein Expression to Circulative Polerovirus Transmission

The Postmitotic Growth Suppressor Necdin Interacts with a Calcium-binding Protein (NEFA) in Neuronal Cytoplasm

Contact Info

Product

Resources

About