Nudel functions in membrane traffic mainly through association with Lis1 and cytoplasmic dynein

Yun Liang, Wei Yu, Yan Li, Zhenye Yang, Xiumin Yan, Qiongping Huang, Xueliang Zhu

Research output: Contribution to journalArticlepeer-review

105 Scopus citations


Nudel and Lis1 appear to regulate cytoplasmic dynein in neuronal migration and mitosis through direct interactions. However, whether or not they regulate other functions of dynein remains elusive. Herein, overexpression of a Nudel mutant defective in association with either Lis1 or dynein heavy chain is shown to cause dispersions of membranous organelles whose trafficking depends on dynein. In contrast, the wild-type Nudel and the double mutant that binds to neither protein are much less effective. Time-lapse microscopy for lysosomes reveals significant reduction in both frequencies and velocities of their minus end-directed motions in cells expressing the dynein-binding defective mutant, whereas neither the durations of movement nor the plus end-directed motility is considerably altered. Moreover, silencing Nudel expression by RNA interference results in Golgi apparatus fragmentation and cell death. Together, it is concluded that Nudel is critical for dynein motor activity in membrane transport and possibly other cellular activities through interactions with both Lis1 and dynein heavy chain.

Original languageEnglish (US)
Pages (from-to)557-566
Number of pages10
JournalJournal of Cell Biology
Issue number4
StatePublished - Feb 16 2004
Externally publishedYes


  • Motility
  • NudE
  • Organelle
  • RNA interference
  • Time-lapse microscopy

ASJC Scopus subject areas

  • Cell Biology


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