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Drosophila Dscam Is an Axon Guidance Receptor Exhibiting Extraordinary Molecular Diversity
Use of double-stranded RNA interference in Drosophila cell lines to dissect signal transduction pathways.
We demonstrate the efficacy of double-stranded RNA-mediated interference (RNAi) of gene expression in generating "knock-out" phenotypes for specific proteins in several Drosophila cell lines. We…
Insights into Lafora disease: malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin.
- Matthew S. Gentry, C. Worby, J. Dixon
- BiologyProceedings of the National Academy of Sciences…
- 14 June 2005
It is demonstrated that malin is a single subunit E3 ubiquitin (Ub) ligase and that its RING domain is necessary and sufficient to mediate ubiquitination, and that lafor in is a physiologic substrate of malin.
Secreted Kinase Phosphorylates Extracellular Proteins That Regulate Biomineralization
Fam20C appears to be the Golgi casein kinase that phosphorylates secretory pathway proteins within S-x-E motifs, and is thus a protein kinase dedicated to the phosphorylation of extracellular proteins.
The fic domain: regulation of cell signaling by adenylylation.
Sorting out the cellular functions of sorting nexins
The authors would like to apologize for the following omissions: the following reference should have been included in the reference list: Ref. 92, references 92 and 92.
Malin Decreases Glycogen Accumulation by Promoting the Degradation of Protein Targeting to Glycogen (PTG)*
- C. Worby, Matthew S. Gentry, J. Dixon
- Biology, ChemistryJournal of Biological Chemistry
- 15 February 2008
Overexpression of PTG markedly increases glycogen accumulation, and decreased PTG expression decreases glycogen stores, suggesting an additional mechanism, involving laforin and malin, in regulating glycogen metabolism.
A Novel Link between Fic (Filamentation Induced by cAMP)-mediated Adenylylation/AMPylation and the Unfolded Protein Response*
It is demonstrated that HYPE localizes to the lumen of the endoplasmic reticulum via its hydrophobic N terminus and adenylylates the ER molecular chaperone, BiP, at Ser-365 and Thr-366, and enhances BiP's ATPase activity, which is required for refolding misfolded proteins while coping with ER stress.
Mitochondrial phosphatase PTPMT1 is essential for cardiolipin biosynthesis.
Laforin, a Dual Specificity Phosphatase That Dephosphorylates Complex Carbohydrates*
It is hypothesized that laforin is unique in its ability to utilize a phosphorylated complex carbohydrate as a substrate and that this function may be necessary for the maintenance of normal cellular glycogen.