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Multiple mechanisms, including lysosomal degradation, control the levels of HIF1a protein. Here we show that HIF1a protein degradation is resistant to lysosomal inhibition and that HIF1a is associated with the Golgi compartment in melanoma cells. Although pharmacological inhibitors of prolyl hydroxylation, neddylation and the proteasome inhibited degradation of HIF1a, attenuation of lysosomal activity with chloroquine did not alter the levels of HIF1a or its association with Golgi. Pharmacological disruption of Golgi resulted in nuclear accumulation of HIF1a. However, blockade of ER\u2010Golgi protein transport in hypoxia reduced the transcript levels of HIF1a target genes. These findings suggest a possible role for the oxygen\u2010dependent protein folding process from the ER\u2010Golgi compartment in fine\u2010tuning HIF1a transcriptional output. J. Cell. Biochem. 117: 853\u2013859, 2016. \u00a9 2015 Wiley Periodicals, Inc.<\/jats:p><\/jats:sec>","DOI":"10.1002\/jcb.25381","type":"journal-article","created":{"date-parts":[[2015,9,16]],"date-time":"2015-09-16T12:54:47Z","timestamp":1442408087000},"page":"853-859","source":"Crossref","is-referenced-by-count":10,"title":["Golgi Associated HIF1a Serves as a Reserve in Melanoma Cells"],"prefix":"10.1002","volume":"117","author":[{"given":"Alexander J.","family":"Lakhter","sequence":"first","affiliation":[{"name":"Department of Dermatology Indiana University School of Medicine Indianapolis Indiana 46202"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tim","family":"Lahm","sequence":"additional","affiliation":[{"name":"Department of Medicine Indiana University School of Medicine Indianapolis Indiana 46202"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hal E.","family":"Broxmeyer","sequence":"additional","affiliation":[{"name":"Department of 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