<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>21(1)</volume><submitter>Stark M</submitter><pubmed_abstract>&lt;h4>Background&lt;/h4>Folates are crucial for the biosynthesis of nucleotides and amino acids, essential for cell proliferation and development. Folate deficiency induces DNA damage, developmental defects, and tumorigenicity. The obligatory enzyme folylpolyglutamate synthetase (FPGS) mediates intracellular folate retention via cytosolic and mitochondrial folate polyglutamylation. Our previous paper demonstrated the association of the cytosolic FPGS (cFPGS) with the cytoskeleton and various cell protrusion proteins. Based on these recent findings, the aim of the current study was to investigate the potential role of cFPGS at cell protrusions.&lt;h4>Results&lt;/h4>Here we uncovered a central role for two G-quadruplex (GQ) motifs in the 3'UTR of FPGS mediating the localization of cFPGS mRNA and protei</pubmed_abstract><journal>BMC biology</journal><pagination>13</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9889130</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Folylpolyglutamate synthetase mRNA G-quadruplexes regulate its cell protrusion localization and enhance a cancer cell invasive phenotype upon folate repletion.</pubmed_title><pmcid>PMC9889130</pmcid><pubmed_authors>Assaraf YG</pubmed_authors><pubmed_authors>Stark M</pubmed_authors><pubmed_authors>Ulitsky I</pubmed_authors><pubmed_authors>Levin M</pubmed_authors></additional><is_claimable>false</is_claimable><name>Folylpolyglutamate synthetase mRNA G-quadruplexes regulate its cell protrusion localization and enhance a cancer cell invasive phenotype upon folate repletion.</name><description>&lt;h4>Background&lt;/h4>Folates are crucial for the biosynthesis of nucleotides and amino acids, essential for cell proliferation and development. Folate deficiency induces DNA damage, developmental defects, and tumorigenicity. The obligatory enzyme folylpolyglutamate synthetase (FPGS) mediates intracellular folate retention via cytosolic and mitochondrial folate polyglutamylation. Our previous paper demonstrated the association of the cytosolic FPGS (cFPGS) with the cytoskeleton and various cell protrusion proteins. Based on these recent findings, the aim of the current study was to investigate the potential role of cFPGS at cell protrusions.&lt;h4>Results&lt;/h4>Here we uncovered a central role for two G-quadruplex (GQ) motifs in the 3'UTR of FPGS mediating the localization of cFPGS mRNA and protei</description><dates><release>2023-01-01T00:00:00Z</release><publication>2023 Feb</publication><modification>2026-07-16T21:51:38.261Z</modification><creation>2025-04-20T02:56:11.026Z</creation></dates><accession>S-EPMC9889130</accession><cross_references><pubmed>36721160</pubmed><doi>10.1186/s12915-023-01525-1</doi></cross_references></HashMap>