Publications by authors named "Ololade Fatunmbi"
The dynamics and organization of the actin cytoskeleton are crucial to many cellular events such as motility, polarization, cell shaping, and cell division. The intracellular and extracellular signaling associated with this cytoskeletal network is communicated through cell membranes. Hence the organization of membrane macromolecules and actin filament assembly are highly interdependent.
View Article and Find Full Text PDFSpatial and temporal control of actin polymerization is fundamental for many cellular processes, including cell migration, division, vesicle trafficking, and response to agonists. Many actin-regulatory proteins interact with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P) and are either activated or inactivated by local PI(4,5)P concentrations that form transiently at the cytoplasmic face of cell membranes. The molecular mechanisms of these interactions and how the dozens of PI(4,5)P-sensitive actin-binding proteins are selectively recruited to membrane PI(4,5)P pools remains undefined.
View Article and Find Full Text PDFArticle Synopsis
- Haptoglobin (Hp) binds free hemoglobin dimers to prevent harmful effects in the body, but there isn't much research on its interaction with myoglobin (Mb), even though they are similar proteins.
- Using computational biology and electrospray ionization mass spectrometry (ESI-MS), the study predicts and tests how Hp interacts with monomeric globins like Mb.
- Findings show that while Mb can bind to Hp, especially at the α-chain site, it does so less efficiently than Hb, indicating that the binding affinity is lower due to differing electrostatic interactions.