期刊
MOLECULAR AND CELLULAR ENDOCRINOLOGY
卷 359, 期 1-2, 页码 2-12出版社
ELSEVIER IRELAND LTD
DOI: 10.1016/j.mce.2011.06.030
关键词
Activin; Inhibin; Transforming growth factor-beta; Follistatin; Betaglycan; Prodomain
Like other members of the transforming growth factor-beta (TGF-beta) superfamily, activins are synthesised as precursor molecules comprising an N-terminal prodomain and C-terminal mature region. During synthesis, the prodomain interacts non-covalently with mature activin, maintaining the molecule in a conformation competent for dimerisation. Dimeric precursors are cleaved by proprotein convertases and activin is secreted from the cell non-covalently associated with its propeptide. Extracellularly, the propeptide interacts with heparan sulfate proteoglycans to regulate activin localization within tissues. The mature activin dimer exhibits the classic 'open-hand' structure of TGF-beta ligands with 'finger-like' domains projecting outward from the cysteine knot core of the molecule. These finger domains form the binding epitopes for type I and II serine/threonine kinase receptors. Activins ability to access its signalling receptors is regulated by the extracellular binding proteins, follistatin, follistatin-like-3, and by inhibins, which, in the presence of betaglycan, sequester type II receptors. (C) 2011 Elsevier Ireland Ltd. All rights reserved.
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