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Tumour suppressors

The stabilizing influence of VHL

Nature Reviews Cancer volume 3, page 4 (2003)Cite this article

So far, the best-characterized function of VHL has been as a component of an E3 ubiquitin ligase complex, which mediates degradation of the hypoxia-inducible factor (HIF) under normoxic conditions. Although there are some links between this and particular subtypes of VHL disease, the extent to which this function of VHL contributes to tumour progression is unclear. More recently, VHL has also been implicated in extracellular-matrix formation and cell-cycle progression.

The importance of the new work from Krek and colleagues is that they identify a novel cytoskeletal function, which is specific to an isoform of VHL that has not previously been linked to VHL tumour development. VHL exists as two isoforms: the longer VHL30 isoform and the shorter VHL19 isoform that results from internal initiation at methionine 54. By raising antibodies that are specific for each isoform, Krek and colleagues revealed that, whereas the shorter isoform localizes predominantly to the nucleus, the longer VHL30 isoform co-localizes with the cytoplasmic microtubule network and depends on an intact microtubule network for this.

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References

ORIGINAL RESEARCH PAPER

  1. Hergovich, A. et al. Regulation of microtubule stability by the von Hippel–Lindau tumour suppressor protein pVHL. Nature Cell Biology 4, 64–70 (2003)

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FURTHER READING

  1. Kaelin, W. G. Jr. Molecular basis of the VHL hereditary cancer syndrome. Nature Rev. Cancer 2, 673–682 (2002).

    Article  CAS  Google Scholar 

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  1. Associate Editor, Nature Cell Biology,

    Alison Schuldt

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  1. Alison Schuldt
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Schuldt, A. The stabilizing influence of VHL. Nat Rev Cancer 3, 4 (2003). https://doi.org/10.1038/nrc976

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