{'fraction_non_alphanumeric': 0.016483516483516484, 'fraction_numerical': 0.0018315018315018315, 'mean_word_length': 5.917721518987341, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Subcellular Localization of The Enzymes In Serine Biosynthesis

Serine biosynthesis uses 3‐phosphoglycerate, an intermediate of glycolysis, to catalyze the first reaction by phosphoglycerate dehydrogenase (PHGDH). This reaction produces 3‐phosphohydroxypyruvate, which eventually becomes serine through two additional steps. Upregulation of serine biosynthesis has been characterized as a hallmark of cancer cell metabolism, as serine is an essential metabolite that provides precursors for various building blocks supporting cancer cell growth and proliferation. We hypothesize that the enzymes involved in serine biosynthesis may associate with each other in the cytoplasm of human cancer cells. To test this hypothesis, we use molecular cloning techniques to tag human PHGDH and others with a fluorescent protein. We will then transfect the plasmids into human cancer cells to examine the localization of PHGDH and others using fluorescent live‐cell imaging. Ultimately, we will contribute to our understanding of the spatiotemporal regulation of serine biosynthesis in human cancer cells.