Tyrosine phosphorylation on DCBLD2 inhibits cell proliferation promoted by PDGFR.
Conference Year
2024
Abstract
Receptors play a crucial role in interacting with the extracellular environment, regulating normal cell development. PDGFRß is a receptor linked to abnormal growth and tumorigenesis, while DCBLD2 is a newly discovered receptor with emerging roles in modulating PDGFRß receptor signaling to prevent proliferation. We propose that phosphorylation of DCBLD2 prompts the downregulation of PDGFRß. Using HEK 293 cell culture, Western Blot, and Mass Spectrometry, we demonstrate that PDGFRß phosphorylates DCBLD2 at 7 intracellular tyrosines, which is essential for inhibiting proliferation. This highlights the importance of tyrosine phosphorylation in receptor-coreceptor interactions in modulating growth and proliferation signals.
Primary Faculty Mentor Name
Bryan Ballif
Status
Graduate
Student College
College of Arts and Sciences
Program/Major
Biology
Primary Research Category
Life Sciences
Tyrosine phosphorylation on DCBLD2 inhibits cell proliferation promoted by PDGFR.
Receptors play a crucial role in interacting with the extracellular environment, regulating normal cell development. PDGFRß is a receptor linked to abnormal growth and tumorigenesis, while DCBLD2 is a newly discovered receptor with emerging roles in modulating PDGFRß receptor signaling to prevent proliferation. We propose that phosphorylation of DCBLD2 prompts the downregulation of PDGFRß. Using HEK 293 cell culture, Western Blot, and Mass Spectrometry, we demonstrate that PDGFRß phosphorylates DCBLD2 at 7 intracellular tyrosines, which is essential for inhibiting proliferation. This highlights the importance of tyrosine phosphorylation in receptor-coreceptor interactions in modulating growth and proliferation signals.