Journal
EMBO JOURNAL
Volume 22, Issue 7, Pages 1555-1566Publisher
OXFORD UNIV PRESS
DOI: 10.1093/emboj/cdg156
Keywords
activin; ActRIIB; TGF-beta; receptors; signaling; structure
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Funding
- NIA NIH HHS [T32 AG000260, T32 AG00260] Funding Source: Medline
- NIGMS NIH HHS [F32 GM65717-01, F32 GM065717] Funding Source: Medline
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The TGF-beta superfamily of ligands and receptors stimulate cellular events in diverse processes ranging from cell fate specification in development to immune suppression. Activins define a major subgroup of TGF-beta ligands that regulate cellular differentiation, proliferation, activation and apoptosis. Activins signal through complexes formed with type I and type II serine/threonine kinase receptors. We have solved the crystal structure of activin A bound to the extracellular domain of a type II receptor, ActRIIB, revealing the details of this interaction. ActRIIB binds to the outer edges of the activin finger regions, with the two receptors juxtaposed in close proximity, in a mode that differs from TGF-beta3 binding to type II receptors. The dimeric activin A structure differs from other known TGF-beta ligand structures, adopting a compact folded-back conformation. The crystal structure of the complex is consistent with recruitment of two type I receptors into a close packed arrangement at the cell surface and suggests that diversity in the conformational arrangements of TGF-beta ligand dimers could influence cellular signaling processes.
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