<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><submitter>Uchida K</submitter><funding>Japan Society for the Promotion of Science</funding><pubmed_abstract>Protein lipidation, particularly palmitoylation (attachment of a 16-carbon fatty acid), regulates cellular behaviors by controlling protein function at lipid membranes. In this study, we prepared a series of lipidated green fluorescent proteins ("EGFP-lipids") with various alkyl chain lengths (C8 to C22). Using model lipid membranes and Jurkat (human T lymphocyte) cells, we evaluated how lipidation affects the membrane interactions and vesicular transport from the membrane of these protein-lipid constructs. Our findings demonstrate that elongation of the alkyl chain profoundly affects both lateral membrane diffusion and vesicular transport of the EGFP-lipids. Only artificially lipidated proteins that mimic &lt;i>in vivo&lt;/i> lipidation exhibited cellular dynamics in response to external signal</pubmed_abstract><journal>RSC chemical biology</journal><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12351397</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Exploring the significance of palmitoylation using an artificial protein lipidation system.</pubmed_title><pmcid>PMC12351397</pmcid><funding_grant_id>JP23KJ1739</funding_grant_id><funding_grant_id>JP19H00841</funding_grant_id><funding_grant_id>JP23H00247</funding_grant_id><pubmed_authors>Shimokawa N</pubmed_authors><pubmed_authors>Shiomoto S</pubmed_authors><pubmed_authors>Goto M</pubmed_authors><pubmed_authors>Uchida K</pubmed_authors><pubmed_authors>Wakabayashi R</pubmed_authors><pubmed_authors>Kamiya N</pubmed_authors><pubmed_authors>Toyofuku K</pubmed_authors><pubmed_authors>Ogushi N</pubmed_authors><pubmed_authors>Tanaka M</pubmed_authors><pubmed_authors>Takagi M</pubmed_authors></additional><is_claimable>false</is_claimable><name>Exploring the significance of palmitoylation using an artificial protein lipidation system.</name><description>Protein lipidation, particularly palmitoylation (attachment of a 16-carbon fatty acid), regulates cellular behaviors by controlling protein function at lipid membranes. In this study, we prepared a series of lipidated green fluorescent proteins ("EGFP-lipids") with various alkyl chain lengths (C8 to C22). Using model lipid membranes and Jurkat (human T lymphocyte) cells, we evaluated how lipidation affects the membrane interactions and vesicular transport from the membrane of these protein-lipid constructs. Our findings demonstrate that elongation of the alkyl chain profoundly affects both lateral membrane diffusion and vesicular transport of the EGFP-lipids. Only artificially lipidated proteins that mimic &lt;i>in vivo&lt;/i> lipidation exhibited cellular dynamics in response to external signal</description><dates><release>2025-01-01T00:00:00Z</release><publication>2025 Aug</publication><modification>2026-05-28T04:14:27.089Z</modification><creation>2026-04-08T02:15:43.02Z</creation></dates><accession>S-EPMC12351397</accession><cross_references><pubmed>40821863</pubmed><doi>10.1039/d5cb00143a</doi></cross_references></HashMap>