PMC:4635215 / 13720-14860 JSONTXT

{"project":"TEST0","denotations":[{"id":"26594142-179-187-125979","span":{"begin":179,"end":183},"obj":"[\"16545397\"]"},{"id":"26594142-184-192-125980","span":{"begin":370,"end":374},"obj":"[\"24639524\"]"},{"id":"26594142-234-242-125981","span":{"begin":1036,"end":1040},"obj":"[\"26280122\"]"}],"text":"In cell and animal models of Alzheimer's disease, increased Aβ processing from the amyloid precursor protein (APP) leads to Golgi fragmentation before cell death (Gonatas et al., 2006). A recent study shows that phosphorylation of GRASP65 by Cdk5 activated by Aβ (possibly through calcium signaling) results in reversible disassembly of the Golgi complex (Joshi et al., 2014). By contrast to other situations where Golgi fragmentation results in decreased cargo trafficking, the Wang group has shown that Aβ-induced fragmentation actually increases cargo trafficking. This results either directly or indirectly in positive feedback, where production of Aβ is increased and thus increases Golgi fragmentation. However, increased Aβ processing may block further accumulation of Aβ. It was recently shown that the intracellular domain of APP (released after Aβ processing and translocated to the nucleus) leads to reduced levels of machinery required for APP trafficking out of the Golgi, and thus reduced production of Aβ (Ceglia et al., 2015). Clearly, there is still much to learn about the role of the Golgi complex in Alzheimer's disease."}

{"project":"0_colil","denotations":[{"id":"26594142-16545397-125979","span":{"begin":179,"end":183},"obj":"16545397"},{"id":"26594142-24639524-125980","span":{"begin":370,"end":374},"obj":"24639524"},{"id":"26594142-26280122-125981","span":{"begin":1036,"end":1040},"obj":"26280122"}],"text":"In cell and animal models of Alzheimer's disease, increased Aβ processing from the amyloid precursor protein (APP) leads to Golgi fragmentation before cell death (Gonatas et al., 2006). A recent study shows that phosphorylation of GRASP65 by Cdk5 activated by Aβ (possibly through calcium signaling) results in reversible disassembly of the Golgi complex (Joshi et al., 2014). By contrast to other situations where Golgi fragmentation results in decreased cargo trafficking, the Wang group has shown that Aβ-induced fragmentation actually increases cargo trafficking. This results either directly or indirectly in positive feedback, where production of Aβ is increased and thus increases Golgi fragmentation. However, increased Aβ processing may block further accumulation of Aβ. It was recently shown that the intracellular domain of APP (released after Aβ processing and translocated to the nucleus) leads to reduced levels of machinery required for APP trafficking out of the Golgi, and thus reduced production of Aβ (Ceglia et al., 2015). Clearly, there is still much to learn about the role of the Golgi complex in Alzheimer's disease."}

{"project":"2_test","denotations":[{"id":"26594142-16545397-38084451","span":{"begin":179,"end":183},"obj":"16545397"},{"id":"26594142-24639524-38084452","span":{"begin":370,"end":374},"obj":"24639524"},{"id":"26594142-26280122-38084453","span":{"begin":1036,"end":1040},"obj":"26280122"}],"text":"In cell and animal models of Alzheimer's disease, increased Aβ processing from the amyloid precursor protein (APP) leads to Golgi fragmentation before cell death (Gonatas et al., 2006). A recent study shows that phosphorylation of GRASP65 by Cdk5 activated by Aβ (possibly through calcium signaling) results in reversible disassembly of the Golgi complex (Joshi et al., 2014). By contrast to other situations where Golgi fragmentation results in decreased cargo trafficking, the Wang group has shown that Aβ-induced fragmentation actually increases cargo trafficking. This results either directly or indirectly in positive feedback, where production of Aβ is increased and thus increases Golgi fragmentation. However, increased Aβ processing may block further accumulation of Aβ. It was recently shown that the intracellular domain of APP (released after Aβ processing and translocated to the nucleus) leads to reduced levels of machinery required for APP trafficking out of the Golgi, and thus reduced production of Aβ (Ceglia et al., 2015). Clearly, there is still much to learn about the role of the Golgi complex in Alzheimer's disease."}