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Technical Report
Loss-of-Function in the DeltaRF Allele Is Due to a Failure of the Delta Protein to Reach the Cell Surface
Anton Delwig and Matthew D. Rand
volume 1 | issue 3
May/June 2007Pages: 190 - 193
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Endocytosis of the Delta ligand presumably drives "trans-endocytosis" of Notch resulting in proteolytic activation of the receptor. This model is founded in Delta mutants that reportedly fail to undergo endocytosis. One such allele, DlRF, gives a temperature-sensitive loss-of-function, purported to be an endocytosis mutant. Here we show that in lineages of Delta-expressing larval neurons the DlRF protein fails to localize to neurites consistent with a failure in trafficking to the plasma membrane. We find that the DlRF allele carries two mutations, G305E and C348Y, in the extracellular epidermal growth factor-like (EGF) repeats 3 and 4. Co-expression of GFP-tagged DlRF and RFP-tagged wild-type Delta (DlWT) in S2 cells demonstrates complete segregation of the proteins at 30ºC with DlRF failing to localize to the plasma membrane. As well, DlRF fails to undergo a characteristic proteolytic processing. Altogether the data indicate that the DlRF allele has limited utility for studying Delta endocytosis mechanisms but is well suited as a tool for loss-of-function studies.
Authors
Anton Delwig
Department of Anatomy and Neurobiology, University of Vermont, Burlington, VT
Matthew D. Rand
Department of Anatomy and Neurobiology, University of Vermont, Burlington, VT
We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link:
Download PDF If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.