First published online April 25, 2008
Development 135, 101e (2008)
© The Company of Biologists Limited
Patterning needs a little sweetener
N-linked glycosylation is a protein modification needed for protein folding
in the endoplasmic reticulum (ER). If unfolded proteins accumulate in the ER,
then the `unfolded protein response' (UPR) is triggered, increasing folding
rates and reducing translation rates. On
p. 1745, Mattias
Mannervik and colleagues describe the first embryonic patterning defects known
to be caused by an inappropriate UPR. In their screen for maternal factors
involved in embryonic patterning, they discovered a mutant -
wollknäuel (wol) - that has reduced Dpp signalling,
posterior segmentation defects due to a lack of the transcription factor
Caudal, and defects in germband elongation and retraction. wol
encodes ALG5, a UDP-glucose:dolichyl-phosphate glucosyltransferase involved in
N-linked glycosylation, and its mutation causes the accumulation of
unglycosylated proteins and triggers the UPR. One component of the UPR is the
phosphorylation of the translation initiation factor eIF2
, which
attenuates protein translation. These findings suggest that some mRNAs, such
as caudal, are particularly sensitive to eIF2
phosphorylation,
resulting in the wol patterning defects.

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Related articles in Development:
- Wollknäuel is required for embryo patterning and encodes the Drosophila ALG5 UDP-glucose:dolichyl-phosphate glucosyltransferase
- Achim Haecker, Mattias Bergman, Christine Neupert, Bernard Moussian, Stefan Luschnig, Markus Aebi, and Mattias Mannervik
Development 2008 135: 1745-1749.
[Abstract]
[Full Text]