Publications by authors named "G Powis"
Article Synopsis
- The pleckstrin homology (PH) domain is a common structural component found in over 250 human proteins, with about 25% having multiple PH domains or being split by other protein domains while still functioning.
- PH domains play significant roles in various human diseases, including cancer and neurodegeneration, and can be modulated through specific pharmacological approaches.
- Recent advances in understanding PH domain structure have led to the development of targeted inhibitors that show promise in treating conditions like cancer and proteus syndrome, with more potential therapies in the works.
Article Synopsis
- Plekha7 is a protein that helps cells stick together and keep strong barriers, which is important for cell health, especially in the lining of the intestines.
- In colorectal cancer, levels of Plekha7 are higher than normal and increase as the cancer gets worse.
- Plekha7 works better with normal KRas proteins than with mutated ones, and stopping Plekha7 can slow down the growth of tumors caused by mutated KRas.
PLEKHA7 (pleckstrin homology domain containing family A member 7) plays key roles in intracellular signaling, cytoskeletal organization, and cell adhesion, and is associated with multiple human cancers. The interactions of its pleckstrin homology (PH) domain with membrane phosphatidyl-inositol-phosphate (PIP) lipids are critical for proper cellular localization and function, but little is known about how PLEKHA7 and other PH domains interact with membrane-embedded PIPs. Here we describe the structural basis for recognition of membrane-bound PIPs by PLEHA7.
View Article and Find Full Text PDFHypoxic solid tumors induce the stabilization of hypoxia-inducible factor 1 alpha (HIF1α), which stimulates the expression of many glycolytic enzymes and hypoxia-responsive genes. A high rate of glycolysis supports the energetic and material needs for tumors to grow. Fructose-1,6-bisphosphate aldolase A (ALDOA) is an enzyme in the glycolytic pathway that promotes the expression of HIF1α.
View Article and Find Full Text PDFHuman cysteine cathepsins constitute an 11-membered family of proteases responsible for degradation of proteins in cellular endosomal-lysosomal compartments as such, they play important roles in antigen processing, cellular stress signaling, autophagy, and senescence. Moreover, for many years these enzymes were also linked to tumor growth, invasion, angiogenesis and metastasis when upregulated. Individual biological roles of each cathepsin are difficult to establish, because of their redundancy and similar substrate specificities.
View Article and Find Full Text PDF