Cell Biology Commons^™

Id2 Complexes With The Snag Domain Of Snai1 Inhibiting Snai1-Mediated Repression Of Integrin Beta4, Cheng Chang, Xiaofang Yang, Bryan Pursell, Arthur M. Mercurio

Arthur M. Mercurio

The epithelial-mesenchymal transition (EMT) is a fundamental process that underlies development and cancer. Although the EMT involves alterations in the expression of specific integrins that mediate stable adhesion to the basement membrane, such as alpha6beta4, the mechanisms involved are poorly understood. Here, we report that Snai1 inhibits beta4 transcription by increasing repressive histone modification (trimethylation of histone H3 at K27 [H3K27Me3]). Surprisingly, Snai1 is expressed and localized in the nucleus in epithelial cells, but it does not repress beta4. We resolved this paradox by discovering that Id2 complexes with the SNAG domain of Snai1 on the beta4 promoter and constrains ...

Use Of Photobiomodulation In Osteoclast Formation: Possible Intervention For The Treatment Of Osteoporosis, Lisa Lauren Anderson-Antle

Theses and Dissertations

After critically examining the literature to gain a robust understanding for the pathogenesis of bone loss, specifically osteoporosis, the development of a possible new intervention to prevent or treat osteoporosis was explored. The purpose of this dissertation was to pilot test a new protocol designed to answer the broad research question: Does Near-Infrared Light Emitting Diode (NIR-LED) treatment affect Receptor Activator of Nuclear Factor Kappa-B Ligand (RANKL) induced osteoclastogenesis in a cell culture model?

Osteoporosis is defined as a disease characterized by low bone mass and structural deterioration of bone tissue, leading to bone fragility and an increased susceptibility to ...

N-Linked Glycosylation Of The Bone Morphogenetic Protein Receptor Type 2 (Bmpr2) Enhances Ligand Binding, Jonathan W. Lowery Ph.D., Jose M Amich, Alex Andonian, Vicki Rosen

Faculty Publications and Research

The bone morphogenetic protein (BMP) signaling pathway is essential for normal development and tissue homeostasis. BMP signal transduction occurs when ligands interact with a complex of type 1 and type 2 receptors to activate downstream transcription factors. It is well established that a single BMP receptor may bind multiple BMP ligands with varying affinity, and this has been largely attributed to conformation at the amino acid level. However, all three type 2 BMP receptors (BMPR2, ACVR2A/B) contain consensus N-glycosylation sites in their extracellular domains (ECDs), which could play a role in modulating interaction with ligand. Here, we show a ...