| First Author | Hines RM | Year | 2010 |
| Journal | J Biol Chem | Volume | 285 |
| Issue | 7 | Pages | 4621-8 |
| PubMed ID | 19955568 | Mgi Jnum | J:161679 |
| Mgi Id | MGI:4460857 | Doi | 10.1074/jbc.M109.069849 |
| Citation | Hines RM, et al. (2010) Golgi-specific DHHC zinc finger protein GODZ mediates membrane Ca2+ transport. J Biol Chem 285(7):4621-8 |
| abstractText | 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. |
