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Published online 26 February 2001. doi:10.1083/jcb.152.5.923
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© The Rockefeller University Press, 0021-9525/2001/3/923/ $5.00
The Journal of Cell Biology, Volume 152, Number 5, March 5, 2001 923-934

Original Article

The Golgi-associated Hook3 Protein Is a Member of a Novel Family of Microtubule-binding Proteins

Jason H. Walentaa, Aaron J. Didiera, Xinran Liua, and Helmut Krämera
a Center for Basic Neuroscience and Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, Texas 75390

Correspondence to: Helmut Krämer, Center for Basic Neuroscience and Department of Cell Biology, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX 75235-9111. Tel:(214) 648-1860 Fax:(214) 648-1801 E-mail:kramer{at}utsw.swmed.edu.

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.

Key Words: membrane trafficking, Hook protein, endosomes, brefeldin A, Golgi complex


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