DPM1, the catalytic subunit of dolichol-phosphate-mannose synthase, is tethered to and stabilized on the endoplasmic reticulum membrane by DPM3

doi:10.1074/jbc.M511311200

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Papers In Press, published online ahead of print November 9, 2005
J. Biol. Chem, 10.1074/jbc.M511311200
Submitted on October 18, 2005
Revised on November 9, 2005
Accepted on November 9, 2005

DPM1, the catalytic subunit of dolichol-phosphate-mannose synthase, is tethered to and stabilized on the endoplasmic reticulum membrane by DPM3

Hisashi Ashida, Yusuke Maeda, and Taroh Kinoshita

Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565-0871

Corresponding Author: tkinoshi{at}biken.osaka-u.ac.jp

Dolichol-phosphate-mannose (DPM) synthase is required for synthesis of the glycosylphosphatidylinositol (GPI)-anchor, N-glycan precursor, protein O-mannose and C-mannose. We previously identified DPM3, the third component of this enzyme, which was co-purified with DPM1 and DPM2. Here, we established mutant Chinese hamster ovary (CHO) 2.38 cells that were defective in DPM3. CHO2.38 cells were negative for GPI-anchored proteins and microsomes from these cells showed no detectable DPM synthase activity, indicating that DPM3 is an essential component of this enzyme. A coiled-coil domain near the C-terminus of DPM3 was important for tethering DPM1, the catalytic subunit of the enzyme, to the ER membrane, and therefore critical for enzyme activity. On the other hand, two transmembrane regions in the N-terminal portion of DPM3 showed no specific functions. DPM1 was rapidly degraded by the proteasome in the absence of DPM3. Free DPM1 was strongly associated with the C-terminus of Hsc70-interacting protein (CHIP), a chaperone-dependent E3 ubiquitin ligase, suggesting that DPM1 is ubiquitinated, at least in part, by CHIP.

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