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JCS ePress online publication date 3 May 2005
doi: 10.1242/jcs.02358

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Research Article

tGolgin-1 (p230, golgin-245) modulates Shiga-toxin transport to the Golgi and Golgi motility towards the microtubule-organizing centre


Atsuko Yoshino, Subba Rao Gangi Setty, Clare Poynton, Eileen L. Whiteman, Agnès Saint-Pol, Christopher G. Burd, Ludger Johannes, Erika L. Holzbaur, Michael Koval, J. Michael McCaffery, and Michael S. Marks*
* Author for correspondence (e-mail: marksm{at}mail.med.upenn.edu)

tGolgin-1 (trans-Golgi p230, golgin-245) is a member of a family of large peripheral membrane proteins that associate with the trans-Golgi network (TGN) via a C-terminal GRIP domain. Some GRIP-domain proteins have been implicated in endosome-to-TGN transport but no function for tGolgin-1 has been described. Here, we show that tGolgin-1 production is required for efficient retrograde distribution of Shiga toxin from endosomes to the Golgi. Surprisingly, we also found an indirect requirement for tGolgin-1 in Golgi positioning. In HeLa cells depleted of tGolgin-1, the normally centralized Golgi and TGN membranes were displaced to the periphery, forming 'mini stacks'. These stacks resembled those in cells with disrupted microtubules or dynein-dynactin motor, in that they localized to endoplasmic-reticulum exit sites, maintained their secretory capacity and cis-trans polarity, and were relatively immobile by video microscopy. The mini stacks formed concomitant with a failure of pre-Golgi elements to migrate along microtubules towards the microtubule-organizing centre. The requirement for tGolgin-1 in Golgi positioning did not appear to reflect direct binding of tGolgin-1 to motile pre-Golgi membranes, because distinct Golgi and tGolgin-1-containing TGN elements that formed after recovery of HeLa cells from brefeldin-A treatment moved independently toward the microtubule-organizing centre. These data demonstrate that tGolgin-1 functions in Golgi positioning indirectly, probably by regulating retrograde movement of cargo required for recruitment or activation of dynein-dynactin complexes on newly formed Golgi elements.
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