Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.3.1.24 extracted from

  • Bauer, R.; Voelzmann, A.; Breiden, B.; Schepers, U.; Farwanah, H.; Hahn, I.; Eckardt, F.; Sandhoff, K.; Hoch, M.
    Schlank, a member of the ceramide synthase family controls growth and body fat in Drosophila (2009), EMBO J., 28, 3706-3716 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.24

Cloned(Commentary)

Cloned (Comment) Organism
gene schlank, located on X-chromosome Drosophila melanogaster

Protein Variants

Protein Variants Comment Organism
H215D site-directed mutagenesis, the point mutation, changing a highly conserved histidine 215 into glutamate, in the Lag1 motif, which inhibits ceramide synthase function in the Lass1 and 5. With schlankH215D, an increase in ceramide levels cannot be observed Drosophila melanogaster
additional information construction of larvae carrying transgenic UASschlankRNAi or UASschlankHA in combination with the hsGAL4 driver line. A short heat shock (1 h) induces schlank RNAi knockdown or schlank overexpression. Modulation of schlank activity correlates with the rate of ceramide de novo synthesis Drosophila melanogaster

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane Lass family members contain four to seven predicted transmembrane domains Drosophila melanogaster 16020
-

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
larva
-
 Drosophila melanogaster
-

Subunits

Subunits Comment Organism
More Lass family members contain four to seven predicted transmembrane domains, a catalytic Lag1 motif and most an N-terminal domain showing sequence homology to DNA-binding homeodomains (Hox domain) Drosophila melanogaster

Synonyms

Synonyms Comment Organism
DLag1
-
 Drosophila melanogaster
Drosophila longevitiy assurance gene-1 homologue
-
 Drosophila melanogaster
schlank
-
 Drosophila melanogaster

General Information

General Information Comment Organism
evolution schlank belongs to the ceramide family, schlank falls into the Lass family, phylogenetic tree of Lass family members and TRAM proteins, overview Drosophila melanogaster
malfunction P-element insertions into the DLag1 locus cause defects in larval growth and fat metabolism. Schlank mutants also show reduction of storage fat, which is deposited as triacylglyerols in the fat body. Hemizygous schlank mutants show a delay of larval development and pronounced growth defects, which depend on the strength of the alleles (Figure 1A-C). Mutants carrying the stronger schlankG0349 allele fail to grow in the larval stages, although they feed. After about 3days, these animals die as small larvae, which morphologically correspond in size to first instar larvae. In contrast, hemizygous animals carrying the weaker schlankG0061 allele are developmentally delayed. Phenotypes, overview. Modulation of schlank activity correlates with the rate of ceramide de novo synthesis Drosophila melanogaster
metabolism ceramide synthases use long-chain bases, sphinganine or sphingosine, and FA-CoAs with varying chain length to produce (dihydro)ceramide, which is a precursor metabolite for all sphingolipids Drosophila melanogaster
physiological function schlank is involved in the de novo synthesis of a broad range of ceramides, the key metabolites of sphingolipid biosynthesis. Schlank can positively regulate fatty acid synthesis by promoting the expression of sterol-responsive element-binding protein (SREBP) and SREBP-target genes. It further prevents lipolysis by downregulating the expression of triacylglycerol lipase. Schlank negatively regulates the expression of lipases in the fat body, downregulating lipolysis. Schlank is a regulator of the balance between lipogenesis and lipolysis in Drosophila melanogaster. Schlank can act as a positive regulator of SREBP-dependent lipogenesis in Drosophila larvae. Role for ceramide synthases in regulating body fat metabolism. Schlank has both a maternal and a zygotic supply and explains the residual mRNA and protein activity in schlankG0349-mutant animals Drosophila melanogaster