Receptor serine/threonine kinases are single transmembrane protein receptors with serine/threonine protein kinase activity in the intracellular region, which functions as a heterodimer. It mainly phosphorylates serine or threonine in downstream signaling proteins, introduces extracellular signals into cells, and then achieves various biological functions by affecting gene transcription.
Its main ligand is transforming growth factor-βs. (transforming growth factor-βs, TGF-βs.) family members, including TGF-β1~TGF-β5, these members have similar structures and functions, and have many effects on cells. TGF-β receptors I and II are typical receptor serine/threonine protein kinases, which may be more complex than receptor tyrosine kinases in transmitting extracellular information and require several receptors to work together.
Depending on the cell type, it may inhibit cell proliferation, stimulate extracellular matrix synthesis, stimulate bone formation, attract cells through chemotaxis, and act as an inducing signal during embryonic development.
Serine threonine kinase belongs to protein kinase, which can phosphorylate the OH group of serine or threonine residues. Serine threonine kinases contain Rho kinase, Aurora kinase, AMP kinase, RAF kinase, Polo like kinase, PIM kinase, ATM kinase and other kinases. The cAMP/cGMP, Ca2+/calmodulin and diacylglycerol and multiple chenmical signals can regulate the activity of serine threonine kinases.
Serine Threonine Kinase receptors can regulate cell proliferation, programmed cell death (apoptosis), cell differentiation, and embryonic development. The specific residues to be phosphorylated are selected on the basis of the consensus sequence of residues flanking the phosphoacceptor site, and a given kinase usually phosphorylates an entire family of substrates. Types of serine/threonine kinases include MAP kinases (activated by protein phosphatases), ERK and stress-activated JNK and p38.
Receptor serine/threonine kinases (RSTKs) are a group of related catalytic receptors that includes TGF-β receptors (TGF-βRI-III) and activin receptors (ALK1-7). RSTKs exist as heterodimers of type I and type II receptors and the ligand binding domain is located in the type II receptor. Upon ligand-receptor binding, the type I receptors are recruited to the complex and are phosphorylated by the type II receptor.
1. Di Fiore MM.; et al. Molecular Mechanisms Elicited by d-Aspartate in Leydig Cells and Spermatogonia. Int J Mol Sci. 2016,17(7): E11272.