Golgi-specific DHHC zinc finger protein GODZ mediates membrane Ca2+ transport.

Abstract

The Golgi-specific zinc finger protein GODZ (palmitoyl acyltransferase/DHHC-3) mediates the palmitoylation and post-translational modification of many protein substrates that regulate membrane-protein interactions. Here, we show that GODZ also mediates Ca(2+) transport in expressing Xenopus laevis oocytes. Two-electrode voltage-clamp, fluorescence, and (45)Ca(2+) isotopic uptake determinations demonstrated voltage- and concentration-dependent, saturable, and substrate-inhibitable Ca(2+) transport in oocytes expressing GODZ cRNA but not in oocytes injected with water alone. Moreover, we show that GODZ-mediated Ca(2+) transport is regulated by palmitoylation, as the palmitoyl acyltransferase inhibitor 2-bromopalmitate or alteration of the acyltransferase DHHC motif (GODZ-DHHS) diminished GODZ-mediated Ca(2+) transport by approximately 80%. The GODZ mutation V61R abolished Ca(2+) transport but did not affect palmitoyl acyltransferase activity. Coexpression of GODZ-V61R with GODZ-DHHS restored GODZ-DHHS-mediated Ca(2+) uptake to values observed with wild-type GODZ, excluding an endogenous effect of palmitoylation. Coexpression of an independent palmitoyl acyltransferase (HIP14) with the GODZ-DHHS mutant also rescued Ca(2+) transport. HIP14 did not mediate Ca(2+) transport when expressed alone. Immunocytochemistry studies showed that GODZ and HIP14 co-localized to the Golgi and the same post-Golgi vesicles, suggesting that heteropalmitoylation might play a physiological role in addition to a biochemical function. We conclude that GODZ encodes a Ca(2+) transport protein in addition to its ability to palmitoylate protein substrates.

DOI: 10.1074/jbc.M109.069849

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@article{Hines2010GolgispecificDZ, title={Golgi-specific DHHC zinc finger protein GODZ mediates membrane Ca2+ transport.}, author={Rochelle M. Hines and Rujun Kang and Angela Goytain and Gary A. Quamme}, journal={The Journal of biological chemistry}, year={2010}, volume={285 7}, pages={4621-8} }