Category
Oral - Theoretical Proposal
Description
The mTORC1 pathway is involved in the regulation of cell growth and translation. The pathway has a complex web of activators and inhibitors to activate mTORC1. mTORC1 is regulated via a small GTPase called Rheb, which interacts directly with mTORC1. GTPases are proteins that bind to guanine triphosphate (GTP) or guanine diphosphate (GDP). When it is bound to GTP, it is in its active state and can activate proteins, causing a cascade of effects downstream; however, when a GTPase is bound to GDP, the GTPase is inactive and does not cause any cellular activities to occur. A GTPase breaks a phosphate off of GTP via hydrolysis naturally over time, but a GTPase activating protein (GAP) encourages this hydrolysis to occur more. To switch back from GDP to GTP, the GTPase does not add a phosphate to GDP, but a guanine nucleotide exchange factor (GEF) is used to remove GDP and add a GTP. Rheb and its GAP, TSC1/2, have been widely studied to understand how the variety of regulators of mTORC1 interact with these proteins. Despite this, the GEF of Rheb has yet to be identified. This review broadly analyzes Rheb and mTORC1, their structures, regulations, and interactions, and explores the mystery of the missing GEF for Rheb.
A Review of Rheb Activation of mTORC1 and the Great Mystery of One Missing GEF
Oral - Theoretical Proposal
The mTORC1 pathway is involved in the regulation of cell growth and translation. The pathway has a complex web of activators and inhibitors to activate mTORC1. mTORC1 is regulated via a small GTPase called Rheb, which interacts directly with mTORC1. GTPases are proteins that bind to guanine triphosphate (GTP) or guanine diphosphate (GDP). When it is bound to GTP, it is in its active state and can activate proteins, causing a cascade of effects downstream; however, when a GTPase is bound to GDP, the GTPase is inactive and does not cause any cellular activities to occur. A GTPase breaks a phosphate off of GTP via hydrolysis naturally over time, but a GTPase activating protein (GAP) encourages this hydrolysis to occur more. To switch back from GDP to GTP, the GTPase does not add a phosphate to GDP, but a guanine nucleotide exchange factor (GEF) is used to remove GDP and add a GTP. Rheb and its GAP, TSC1/2, have been widely studied to understand how the variety of regulators of mTORC1 interact with these proteins. Despite this, the GEF of Rheb has yet to be identified. This review broadly analyzes Rheb and mTORC1, their structures, regulations, and interactions, and explores the mystery of the missing GEF for Rheb.
Comments
Undergraduate - 1st Place Award Winner