The Golgi-associated Hook3 protein is a member of a novel family of microtubule-binding proteins

Jason H. Walenta, Aaron J. Didier, Xinran Liu, Helmut Krämer

Research output: Contribution to journalArticle

143 Scopus citations


Microtubules are central to the spatial organization of diverse membrane- trafficking systems. Here, we report that Hook proteins constitute a novel family of cytosolic coiled coil proteins that bind to organelles and to microtubules. The conserved NH2-terminal domains of Hook proteins mediate attachment to microtubules, whereas the more divergent COOH-terminal domains mediate the binding to organelles. Human Hook3 bound to Golgi membranes in vitro and was enriched in the cis-Golgi in vivo. Unlike other cis-Golgi-associated proteins, however, a large fraction of Hook3 maintained its juxtanuclear localization after Brefeldin A treatment, indicating a Golgi-independent mechanism for Hook3 localization. Because overexpression of Hook3 caused fragmentation of the Golgi complex, we propose that Hook3 participates in defining the architecture and localization of the mammalian Golgi complex.

Original languageEnglish (US)
Pages (from-to)923-934
Number of pages12
JournalJournal of Cell Biology
Issue number5
Publication statusPublished - Mar 5 2001



  • Brefeldin A
  • Endosomes
  • Golgi complex
  • Hook protein
  • Membrane trafficking

ASJC Scopus subject areas

  • Cell Biology

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