Sukhbir Kaur,
Staff Scientist,
National Cancer Institute, National Institutes of Health
Dr. Kaur obtained her Ph.D. from Guru Nanak Dev University (Punjab, India) and her post-doctoral fellowship training at Genome Technology branch (NHGR1) where she developed her interest in miRNAs and non-coding RNAs. Later, she became a staff scientist in Biochemical Pathology Section, where she expertise her research in area of extracellular vesicles (Exosomes). Dr. Kaur discovered that CD47, which is known as the “don’t eat me” signal and which is upregulated in many cancers, is also present on exosomes. Her major interest is to explore the role of exosome associated CD47 in breast and prostate cancers. Dr. Kaur has received many awards, including the Director's Innovation Award, the NIH Mentoring Award, and technology transfer awards. She serves on numerous Review panel Groups and co-author of more than 40 scientific publications.
Filamin-A and a4ß1 Integrin are CD47-dependent Cargo Proteins in Extracellular Vesicles
Thursday, 4 April 2024 at 12:30
Add to Calendar ▼2024-04-04 12:30:002024-04-04 13:30:00Europe/LondonFilamin-A and a4ß1 Integrin are CD47-dependent Cargo Proteins in Extracellular VesiclesExtracellular Vesicles (EVs) and Nanoparticles 2024: Diagnostics, Delivery, Therapeutics in Miami, FloridaMiami, FloridaSELECTBIOenquiries@selectbiosciences.com
CD47 is a ubiquitously expressed membrane protein that functions as a receptor for thrombospondin-1 and the counter receptor for signal regulatory protein alpha in phagocytes. CD47 is expressed on a subset of extracellular vesicles (EVs) that contain a distinct population of RNAs {Kaur, 2018 #1}. CD47 colocalizes predominantly with CD81 and a4ß1 integrin on Jurkat T cell-derived EVs but not with classical EVs bearing CD63 or CD9 {Kaur, 2022 #2}. CD47 and its cytoplasmic adapter ubiquilin-1 regulate which RNAs are packaged into T cell EVs via physical interactions with components of the exportin-1/Ran nuclear export complex and its known cargos {Kaur, 2022 #3}. Here, we report that disruption of CD47 in Jurkat T lymphoblast and PC3 prostate carcinoma cells impairs the sorting of filamin A and a4ß1 integrin into EVs. Targeted mass spectrometry and coimmunoprecipitation analyses indicate that CD47 indirectly interacts with filamin A either via ubiquilin-1/Exportin-1 or ß1 Integrin. Filamin A may thereby play an important role in CD47-dependent sorting of protein and RNA cargoes into specific subsets of EVs.
Conclusions: CD47 and ubiquilin-1 interact with filamin A, which is known to interact with the cytoplasmic domain of ß1 integrins to regulate integrin function. Less filamin A and a4ß1 integrin sort into EV in the absence of CD47, suggesting that CD47 promotes filamin A and integrin sorting into EV, mediated through ubiquilin1 and/or exportin-1.
Add to Calendar ▼2024-04-03 00:00:002024-04-04 00:00:00Europe/LondonExtracellular Vesicles (EVs) and Nanoparticles 2024: Diagnostics, Delivery, TherapeuticsExtracellular Vesicles (EVs) and Nanoparticles 2024: Diagnostics, Delivery, Therapeutics in Miami, FloridaMiami, FloridaSELECTBIOenquiries@selectbiosciences.com
Add to Calendar ▼2024-04-04 12:30:002024-04-04 13:30:00Europe/LondonFilamin-A and a4ß1 Integrin are CD47-dependent Cargo Proteins in Extracellular VesiclesExtracellular Vesicles (EVs) and Nanoparticles 2024: Diagnostics, Delivery, Therapeutics in Miami, FloridaMiami, FloridaSELECTBIOenquiries@selectbiosciences.com
