Competition between the golgin Imh1p and the Gcs1p GAP stabilizes activated Arl1p at the late-Golgi.

Golgins play diverse roles in regulating the structure and function of the Golgi. The yeast golgin Imh1p is targeted to the trans-Golgi network (TGN) through interaction of its GRIP domain with GTP-bound Arl1p. Recycling of Arl1p and Imh1p to the cytosol requires the hydrolysis of GTP bound to Arl1p, however, ...
when GTP hydrolysis occurs remains unknown. Here, we report that self-interaction of Imh1p plays a role in modulating spatial inactivation of Arl1p. Deletion of IMH1 in yeast decreases the amount of the GTP-bound Arl1p and results in less Arl1p residing on the TGN. Biochemically, purified Imh1p competes with Gcs1p, an Arl1p GTPase-activating protein (GAP), for binding to Arl1p, thus interfering with the GAP activity of Gcs1p toward Arl1p. Furthermore, we demonstrate that the self-interaction of Imh1p attenuates the Gcs1p-dependent GTP hydrolysis of Arl1p. Thus, we infer that the golgin Imh1p serves as a feedback regulator to modulate the GTP hydrolysis of Arl1p.
Unknown
Date: Jul. 05, 2012
Download Curated Data For This Publication
135875
Switch View:
  • Interactions 8