Activin proteins that belong to the transforming growth factor-beta (TGF-β) superfamily; exert their biological actions by binding to heteromeric receptor complexes of type I and type II serine/threonine kinase receptors. On ligand binding; type I and II receptors form a stable complex; resulting in phosphorylation of type I receptors by type II receptors with constitutive kinase activity; and subsequently initiates the activation of downstream molecules including the endogenous Smads. ActRIIB; also known as ActRIIB; is a type II receptor containing an extracellular domain (ECD); a transmembrane segment; and a cytoplasmic region that includes the kinase domain. ActRIIB is a receptor for activin A; activin B and inhibin A. Multiple ActRIIB isoforms can also be generated; which bind activin isoforms with different affinities.
Activin RIA, also known as ALK-2, TSK-7L, SKR1, TSR-I, and ACTR-I, is a glycosylated 65 kDa type I receptor in the TGF-beta serine/threonine kinase receptor family. Binding of TGF-beta superfamily ligands induces formation of a heterotetrameric complex that contains two chains each of a type I and a type II receptor in multiple combinations. The type II receptors phosphorylate the type I receptors which then phosphorylate and activate Smad signal transduction proteins. Activin RIA functions in a wide variety of growth and differentiation processes including gastrulation, skeletal system development, and cardiac morphogenesis. BMP signaling through Activin RIA is enhanced by the direct interaction between Activin RIA and RGM-B/DRAGON, a BMP coreceptor that also associates with other type I and type II receptors. Activin RIA can additionally phosphorylate the coreceptor Endoglin and is required for the inhibitory effect of Endoglin on prostate cancer cell motility.
Activin Receptor Type-2A is a protein that in humans is encoded by the ACVR2A gene. ACVR2A is an activin type 2 receptor. This gene encodes activin A type II receptor. Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins. Activins signal through a heteromeric complex of receptor serine kinases which include at least two type I (I and IB) and two type II (II and IIB) receptors. These receptors are all transmembrane proteins; composed of a ligand-binding extracellular domain with cysteine-rich region; a transmembrane domain; and a cytoplasmic domain with predicted serine/threonine specificity. Type I receptors are essential for signaling; and type II receptors are required for binding ligands and for expression of type I receptors. Type I and II receptors form a stable complex after ligand binding; resulting in phosphorylation of type I receptors by type II receptors. Type II receptors are considered to be constitutively active kinases.
ACVR2A and ACVR2B are two activin type II receptors. ACVR2A has been shown to interact with INHBA, SYNJ2BP and ACVR1B. The bovine ACVR2A gene encodes a protein of 513 amino acids which is highly homologous (approximately 98% identity) to the rat, mouse, and human ACVR2A proteins. Inactivation of ACVR2A is a common event in prostate cancer cells suggesting it may play an important role in the development of prostate cancer. The ACVR2A gene is a putative tumor suppressor gene that is frequently mutated in microsatellite-unstable colon cancers (MSI-H colon cancers). Frameshift mutation of ACVR2A may contribute to MSI-H colon tumorigenesis via disruption of alternate TGF-beta effector pathways.
F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein.
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