VESICULAR TRAFFICKING OF HSPA1A TO THE PLASMA MEMBRANE OF HEAT-SHOCKED CELLS

VESICULAR TRAFFICKING OF HSPA1A TO THE PLASMA MEMBRANE OF HEAT-SHOCKED CELLS | Zenodo Skip to main Communities My dashboard Log in Sign up Zenodo is currently experiencing slowness and intermittent outages due to heavy automated traffic from bots and AI crawlers. We are aware of the problem, and our team is focused on stabilizing the service. Thank you for your patience. California State University, Fullerton Theses & Dissertations Published May 1, 2026 | Version v1 Thesis Embargoed VESICULAR TRAFFICKING OF HSPA1A TO THE PLASMA MEMBRANE OF HEAT-SHOCKED CELLS Authors/Creators Low, Jia Hua (Jensen) Contributors Supervisor (3): Nikolaidis, Nikolas Jimenez-Ortiz, Veronica Miyamoto, Alison Description HSPA1A is a molecular chaperone that regulates cellular homeostasis under stress and is frequently upregulated in cancer cells. In addition to its cytosolic functions, HSPA1A localizes to the plasma membrane (PM) in stressed and tumor cells, where it is associated with increased cell survival and therapeutic resistance. Despite its importance, the mechanisms underlying HSPA1A translocation to the PM remain poorly understood. Based on previous findings that HSPA1A associates with specific lipids, I hypothesized that its PM localization is mediated through a lipid-dependent vesicular trafficking mechanism. Confocal imaging showed that HSPA1A redistributes across endosomal compartments following heat shock, with increased association with recycling and lysosomal pathways and dynamic localization to phosphoinositide-enriched membranes. Pharmacological perturbation of lipid composition modestly reduced HSPA1A PM localization. Inhibition of ER-Golgi transport had no effect, whereas disruption of endosomal and lysosomal pathways resulted in small but significant reductions, suggesting that multiple vesicular routes contribute to HSPA1A trafficking. Modulation of lysosomal lipid composition and phosphoinositide regulation further demonstrated that BMP levels and Sac1 activity influence HSPA1A PM localization. Together, these findings support a model in which HSPA1A is trafficked to the PM through lipid-dependent vesicular pathways regulated by lipid composition and compartment-specific lipid dynamics. Files Embargoed The files will be made publicly available on June 1, 2028. 31 Views 1 Downloads Show more details All versions This version Views Total views 31 31 Downloads Total downloads 1 1 Data volume Total data volume 2.5 MB 2.5 MB More info on how stats are collected.... Versions External resources Indexed in OpenAIRE Communities Keywords and subjects Keywords heat shock response HSPA1A trafficking lipid-protein interactions endo-lysosomal pathway vesicular transport phosphoinositides Details DOI DOI Badge DOI 10.5281/zenodo.19938527 Markdown [](https://doi.org/10.5281/zenodo.19938527) reStructuredText .. image:: https://zenodo.org/badge/DOI/10.5281/zenodo.19938527.svg :target: https://doi.org/10.5281/zenodo.19938527 HTML <a href="https://doi.org/10.5281/zenodo.19938527"><img src="https://zenodo.org/badge/DOI/10.5281/zenodo.19938527.svg" alt="DOI"></a> Image URL https://zenodo.org/badge/DOI/10.5281/zenodo.19938527.svg Target URL https://doi.org/10.5281/zenodo.19938527 Resource type Thesis Publisher Zenodo Thesis California State University, Fullerton Languages English Rights License Creative Commons Attribution 4.0 International The Creative Commons Attribution license allows re-distribution and re-use of a licensed work on the condition that the creator is appropriately credited. Read more Citation Export Technical metadata Created May 1, 2026 Modified May 1, 2026 Jump up About About Policies Infrastructure Principles Projects Roadmap Contact Blog Blog Support Help FAQ Developers REST API OAI-PMH Contribute GitHub Donate Funded by Powered by CERN Data Centre & InvenioRDM Status Privacy policy Cookie policy Terms of Use This site uses cookies. Find out more on how we use cookies Accept all cookies Accept only essential cookies

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