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Full-Text Articles in Life Sciences
Characterization Of Cofilin And Its Potential Role In The Epha4 Pathway, Brian Donald Condron
Characterization Of Cofilin And Its Potential Role In The Epha4 Pathway, Brian Donald Condron
Master's Theses and Doctoral Dissertations
EphA4 is a receptor tyrosine kinase that is responsible for cellular adhesion and locomotion using repulsion signaling in early development of Xenopus laevis. EphA4 regulates cellular locomotion by controlling proteins within its signal transduction pathway, which may include the protein cofilin. Cofilin actively severs and removes actin monomers, thus altering the actin cytoskeleton, leading to the cessation of cellular crawl. During the gastrulation phase of embryonic development, individual cells are relocating to create the three primary germ layers of the organism. Failure of this process to occur results in attrition of the embryos, frequently by way of embryonic exogastrulation. …
Altering Oligomerization Of Epha2 Via Mutations In The Intracellular Domain, Ryan W. Lingerak
Altering Oligomerization Of Epha2 Via Mutations In The Intracellular Domain, Ryan W. Lingerak
Williams Honors College, Honors Research Projects
Eph receptor tyrosine kinases (RTKs) are activated by membrane-bound ligands called ephrins. Eph RTKs are divided into two subclasses, each activated by a specific classes of the ligand ephrin. The overexpression of Eph receptors is correlated to cancer cell metastasis in several different types of cancers. Studies with the EphA2 extracellular domain (ECD) and ephrinA1 ligand have shown that upon binding of ephrin to the receptor, EphA2 undergoes increased oligomerization and activation. This indicates that oligomerization is intimately connected to kinase activity. High resolution crystal structures of the EphA2 ECD have revealed some details of these ligand bound oligomers, as …