<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Barua D</submitter><funding>NIGMS NIH HHS</funding><pagination>e51669</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3524258</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>7(12)</volume><pubmed_abstract>We present a model of the early events in mast cell signaling mediated by FcεRI where the plasma membrane is composed of many small ordered lipid domains (rafts), surrounded by a non-order region of lipids consisting of the remaining plasma membrane. The model treats the rafts as transient structures that constantly form and breakup, but that maintain a fixed average number per cell. The rafts have a high propensity for harboring Lyn kinase, aggregated, but not unaggregated receptors, and the linker for the activation of T cells (LAT). Phosphatase activity in the rafts is substantially reduced compared to the nonraft region. We use the model to analyze published experiments on the rat basophilic leukemia (RBL)-2H3 cell line that seem to contradict the notion that rafts offer protection. In</pubmed_abstract><journal>PloS one</journal><pubmed_title>A mechanistic model of early FcεRI signaling: lipid rafts and the question of protection from dephosphorylation.</pubmed_title><pmcid>PMC3524258</pmcid><funding_grant_id>R37-GM035556</funding_grant_id><funding_grant_id>R37 GM035556</funding_grant_id><pubmed_authors>Goldstein B</pubmed_authors><pubmed_authors>Barua D</pubmed_authors></additional><is_claimable>false</is_claimable><name>A mechanistic model of early FcεRI signaling: lipid rafts and the question of protection from dephosphorylation.</name><description>We present a model of the early events in mast cell signaling mediated by FcεRI where the plasma membrane is composed of many small ordered lipid domains (rafts), surrounded by a non-order region of lipids consisting of the remaining plasma membrane. The model treats the rafts as transient structures that constantly form and breakup, but that maintain a fixed average number per cell. The rafts have a high propensity for harboring Lyn kinase, aggregated, but not unaggregated receptors, and the linker for the activation of T cells (LAT). Phosphatase activity in the rafts is substantially reduced compared to the nonraft region. We use the model to analyze published experiments on the rat basophilic leukemia (RBL)-2H3 cell line that seem to contradict the notion that rafts offer protection. In</description><dates><release>2012-01-01T00:00:00Z</release><publication>2012</publication><modification>2025-05-29T22:28:56.447Z</modification><creation>2025-05-29T22:28:56.447Z</creation></dates><accession>S-EPMC3524258</accession><cross_references><pubmed>23284735</pubmed><doi>10.1371/journal.pone.0051669</doi></cross_references></HashMap>