MRAS spans a length of 209 amino acid residues. Its N-terminal amino acid sequence shares 60-75% identity with that in the Ras protein, while its effector region is identical to that in Ras . MRAS functions as a molecular switch, cycling between an active GTP-bound state and an inactive GDP-bound state. This switching mechanism is regulated by the addition and removal of a phosphate group .
MRAS is predominantly found in its state 1 conformation, which does not bind Ras effectors . It serves as an important signal transducer for various signaling pathways, including those promoting neural and bone formation as well as tumor growth . MRAS activates the MAP kinase pathway, which is crucial for controlling cell proliferation .
MRAS is ubiquitously expressed in many tissues and cell types . It is involved in multiple signaling pathways, including the tumor necrosis factor-alpha and MAP kinase signaling pathways . The protein is associated with the plasma membrane, intracellular anatomical structures, and the actin cytoskeleton .
Dysregulation of Ras signaling, including MRAS, has been associated with various types of cancer . MRAS is also linked to Noonan Syndrome 11 and Rasopathy . Additionally, the MRAS gene contains one of 27 single nucleotide polymorphisms (SNPs) associated with an increased risk of coronary artery disease .
Human recombinant MRAS is used in research to study its role in cell signaling and its implications in diseases. Understanding the function and regulation of MRAS can provide insights into the development of targeted therapies for conditions associated with its dysregulation.