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Introduction
Biological Introduction
SHOC2-PP1C-MRAS is a human enzyme that is involved in regulating cell proliferation and division[1]. The enzyme is involved in the vast RAS-MAPK pathway, which is initially activated by an extracellular growth factor binding to a membrane bound RAS GTPase[1] such as HRAS, NRAS, or KRAS. RAS-GTPases are a family of proteins that work by functioning as molecular switches. This occurs from the protein alternating between binding GTP to be active and GDP to be inactive [1]. After activation via an extracellular growth factor, the RAS-GTPase enzyme binds GTP, which activates RAF[2].
Structural Introduction
The active holoenzyme contains 3 domains. The SHOC-2(blue), PP1C(coral), and MRAS (green) domains form the complete SMP complex.
SHOC-2 is a scaffolding protein scaffolding protein that holds the other subunits in the correct orientation, allowing for the holoenzyme to be functional.
Biological Function
Relevance
Structural highlights
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- ↑ 1.0 1.1 Bernal Astrain G, Nikolova M, Smith MJ. Functional diversity in the RAS subfamily of small GTPases. Biochem Soc Trans. 2022 Apr 29;50(2):921-933. doi: 10.1042/BST20211166. DOI:10.1042/BST20211166.
- ↑ Molina JR, Adjei AA. The Ras/Raf/MAPK pathway. J Thorac Oncol. 2006 Jan;1(1):7-9. DOI:10.1016/S1556-0864(15)31506-9.