Nek1 phosphorylates von Hippel-Lindau tumor suppressor to promote its proteasomal degradation and ciliary destabilization

Mallikarjun Patil, Navjotsingh Pabla, Shuang Huang, Zheng Dong

Research output: Contribution to journalArticle

12 Scopus citations


Loss of function in either VHL or Nek1 leads to cyst formation in tissues, especially in kidneys. Whether there is a connection between pVHL and Nek1 regulation is unknown. Here, we report that the VHL protein (pVHL) may be a substrate of Nek1. While Nek1 can phosphorylate pVHL at multiple sites, the phosphorylation at serine-168 results in pVHL degradation. Nek1-mediated phosphorylation of pVHL does not significantly affect hypoxia-inducible factors (HIF), a known target of pVHL. However, non-phosphorylable pVHL reconstituted in VHL-deficient cells induces more stable cilia than wild-type VHL during serum stimulation and Nocodazole treatment. The results suggest a possible regulation of pVHL by Nek1 that may contribute to ciliary homeostasis and cystogenesis.

Original languageEnglish (US)
Pages (from-to)166-171
Number of pages6
JournalCell Cycle
Issue number1
Publication statusPublished - Jan 1 2013



  • Cilium
  • Hypoxia-inducible factor
  • Nek1
  • Phosphorylation
  • VHL

ASJC Scopus subject areas

  • Molecular Biology
  • Developmental Biology
  • Cell Biology

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