My journey in the discovery of nucleotide sugar transporters of the Golgi apparatus

Indexación: Scopus.I decided to do a second, 2-year postdoc in Phil Robbins’ lab at MIT. I applied for a 1-year extension of my Jane Coffin Childs Memorial Fund for Medical Research Fellowship and was advised by the director that while this was not unprecedented, I had to convince the Board of Scientific Advisors that I deserved this extra year more than new applicants who had never had a fellowship. I still wince at this, but as luck would have it, I had an ally in Joan Lusk. Joan, as mentioned previously, had been a former student in Kennedy’s lab and had moved on to a postdoc position in Salvador (Salva for short) Luria’s lab at MIT. Luria happened to be on the Board of the Jane Coffin Childs Memorial Fund for Medical Research, and Joan had told him about our cardiolipin synthase results. I was able to get a third year of fundingI had received money, for what amounted to approximately half an NIH grant, from the Jane Coffin Childs Memorial Fund for Medical Research to start up my independent laboratory. Salva wanted to know whether I would return the unspent money to the Fund if I received an NIH grant during the firstChemicals and CAS Registry Numbers: 4,4' diisothiocyanatostilbene 2,2' disulfonic acid, 53005-05-3; adenosine 3' phosphate 5' phosphosulfate, 482-67-7; adenosine triphosphate, 15237-44-2, 56-65-5, 987-65-5; casein, 9000-71-9; edetic acid, 150-43-6, 60-00-4; fucose, 3615-37-0, 3713-31-3; fucosyltransferase, 56626-18-7; glycosyltransferase, 9033-07-2; guanosine diphosphate, 146-91-8; guanosine phosphate, 29593-02-0, 5550-12-9, 85-32-5; mannose, 31103-86-3, 3458-28-4; sphingosine, 123-78-4; Adenosine Triphosphate; Nucleotide Transport Proteins; Nucleotides; SugarsDefects in protein glycosylation can have a dramatic impact on eukaryotic cells and is associated with mental and developmental pathologies in humans. The studies outlined below illustrate how a basic biochemical problem in the mechanisms of protein glycosylation, specifically substrate transporters of nucleotide sugars, including ATP and 3-phosphoadenyl-5-phosphosulfate (PAPS), in the membrane of the Golgi apparatus and endoplasmic reticulum, expanded into diverse biological systems from mammals, including humans, to yeast, roundworms, and protozoa. Using these diverse model systems allowed my colleagues and me to answer fundamental biological questions that enabled us to formulate far-reaching hypotheses and expanded our knowledge of human diseases caused by malfunctions in the metabolic processes involved. © 2018 Hirschberg Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc.http://www.jbc.org/content/293/33/12653.ful