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Full-Text Articles in Biochemistry, Biophysics, and Structural Biology
The Mitochondrial Calcium Uniporter Regulator 1 (Mcur1) Matrix Domain Is A Self-Associated Multimer Sensitive To Divalent Cations, Naveed Siddiqui
The Mitochondrial Calcium Uniporter Regulator 1 (Mcur1) Matrix Domain Is A Self-Associated Multimer Sensitive To Divalent Cations, Naveed Siddiqui
Electronic Thesis and Dissertation Repository
Mitochondria are primarily appreciated for the generation of adenosine triphosphate (ATP), a chemical store of energy required by all cells. These organelles, however, also play key roles in apoptosis, autophagy and shaping cytosolic calcium (Ca2+) signaling via Ca2+ uptake into the mitochondrial matrix. This Ca2+ uptake is mediated chiefly via the mitochondrial Ca2+ uniporter (MCU), an inner mitochondrial membrane protein that oligomerizes to form a Ca2+ selective pore. MCU is regulated by several protein binding partners, including the recently identified MCU regulator-1 (MCUR1). MCUR1 stabilizes a higher order MCU heterocomplex through interactions with MCU …
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 …