期刊
CELL REPORTS
卷 29, 期 13, 页码 4608-+出版社
CELL PRESS
DOI: 10.1016/j.celrep.2019.11.110
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资金
- NIH [RO1GM116860]
- Commonwealth Foundation for Cancer Research
- Center for Experimental Therapeutics at Memorial Sloan Kettering Cancer Center
- Cancer Center Core Support grant from the National Institutes of Health [P30 CA008748]
Attachment of palmitate to the N terminus of Sonic hedgehog (Shh) is essential for Shh signaling. Shh palmitoylation is catalyzed on the luminal side of the endoplasmic reticulum (ER) by Hedgehog acyltransferase (Hhat), an ER-resident enzyme. Palmitoyl-coenzyme A (CoA), the palmitate donor, is produced in the cytosol and is not permeable across membrane bilayers. It is not known how palmitoyl-CoA crosses the ER membrane to access the active site of Hhat. Here, we use fluorescent and radiolabeled palmitoyl-CoA probes to demonstrate that Hhat promotes the uptake of palmitoyl-CoA across the ER membrane in microsomes and semi-intact cells. Reconstitution of purified Hhat into liposomes provided further evidence that palmitoyl-CoA uptake activity is an intrinsic property of Hhat. Palmitoyl-CoA uptake was regulated by and could be uncoupled from Hhat enzymatic activity, implying that Hhat serves a dual function as a palmitoyl acyl-transferase and a conduit to supply palmitoyl-CoA to the luminal side of the ER.
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