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Cell biology

Protein sweetener

Nature volume 415, pages 382–383 (2002)Cite this article

After years of failure, a protein involved in flipping certain oligosaccharide molecules into the endoplasmic reticulum — one of the cellular sites where proteins are modified with sugars — has been tracked down.

There are some well-known biological processes that repeatedly resist attempts to characterize them thoroughly. When they finally succumb, it often turns out that an early observation held the key to the solution. The paper by Helenius and colleagues1 on page 447 of this issue will surely be the key to one such process — how lipid-linked sugar molecules are flipped from the outside to the inside of a cellular compartment known as the endoplasmic reticulum (ER). Such 'oligosaccharide flipping' is needed so that certain newly synthesized proteins can be appropriately tagged with sugar groups (glycosylated). Although this glycosylation initially occurs in the ER, the sugar chains are synthesized on the outside of this compartment, and so need to be transported into it. Helenius et al. provide indirect but compelling evidence that a protein called Rft1 is involved.

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Figure 1: Cellular events that lead to the modification of proteins with sugar groups.

References

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  1. Institute for Biotechnological Research, University of San Martin, CC 30, San Martin, 1650, Argentina

    Armando J. Parodi

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  1. Armando J. Parodi
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Correspondence to Armando J. Parodi.

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Parodi, A. Protein sweetener. Nature 415, 382–383 (2002). https://doi.org/10.1038/415382a

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