BEGIN:VCALENDAR VERSION:2.0 PRODID:Icfo X-PUBLISHED-TTL:P1W BEGIN:VEVENT UID:6ae8ff7302bc8 DTSTART:20261112T140000Z SEQUENCE:0 TRANSP:OPAQUE LOCATION:ICFO Auditorium SUMMARY:ICFO | ROGER PONS LANAU CLASS:PUBLIC DESCRIPTION:The secretory pathway is a crucial process for cellular homeost asis\, responsible for the synthesis\, processing\, and trafficking of app roximately a third of all proteins to their final destinations. Newly synt hesized secretory proteins enter the endoplasmic reticulum (ER) and\, afte r proper folding\, are sorted into and exported from specific ER subdomain s named ER exit sites (ERES). As the first trafficking step\, ER protein e xport plays a crucial role in ensuring the correct flow of proteins to dow nstream compartments\, and defects result in a variety of pathological con ditions. Unraveling its organization in space and time is essential to und erstanding its mechanisms. Despite the origins of this research field dati ng to the late 1960s\, it was not until the widespread adoption of fluores cence microscopy techniques in the past three decades that rapid progress was made in how we conceptualize ER protein export in living cells. Yet\, up until now\, researchers have mostly relied on population-averaged measu rements\, which provide limited information on the molecular heterogeneity inherent in biology. Insights into molecular dynamics\, transient interac tions\, short-lived states\, or nanoscale distribution of secretory pathwa y proteins in living cells have largely remained veiled. Developing a comp lete view requires characterizing the process at the single-molecule level .\nIn this thesis\, we develop and apply a quantitative framework based on single-molecule fluorescence microscopy to dissect the dynamic organizati on of the early secretory pathway at the molecular level. By leveraging re cent technological advances in fluorescent dyes\, functional assays\, gene editing\, and machine learning tools\, our approach enables the detection \, monitoring\, and analysis of individual cargo protein molecules as they are exported from ERES with high spatial precision (~20-30 nm) and tempor al resolution (~10 ms). Our characterization provides novel insights into the orchestration of the early secretory pathway\, allowing us to revisit conflicting ideas in the field. Overall\, this thesis provides a generaliz able methodology and an updated\, more accurate view of a fundamental intr acellular trafficking process.\nThursday November 12\, 15:00 h. ICFO Audit orium Thesis Director: Prof. Dr. Marí\;a Garcí\;a Parajo and D r. Felix Campelo Aubarell DTSTAMP:20261102T212403Z END:VEVENT END:VCALENDAR