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Regulation of activin's access to the cell: why is Mother Nature such a control freak?
Author(s) -
Phillips David J.
Publication year - 2000
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/1521-1878(200008)22:8<689::aid-bies2>3.0.co;2-5
Subject(s) - acvr2b , activin type 2 receptors , activin receptor , follistatin , microbiology and biotechnology , smad , tgf beta signaling pathway , biology , amphiregulin , transforming growth factor , receptor , signal transduction , smad2 protein , growth factor , medicine , biochemistry
Activin A is a pluripotent growth factor with important roles in development, erythropoiesis and the local regulation of many tissues. At the post‐translational level, the amount of activin A produced by cells may be modulated through the diversion of activin A subunits into the formation of inhibin or other activins containing heterodimeric forms. Once assembled, activin interacts with various low‐ and high‐affinity binding proteins, such as follistatin and α 2 ‐macroglobulin, that have consequences for receptor availability. In common with other TGFβ family members, activin signals through pairs of type I and II receptor kinases and the Smad intracellular signalling cascade. Other checkpoints have been identified such as the recently identified pseudoreceptor, BAMBI. These emerging findings point to a tightly coordinated regulation of the exposure of a cell or tissue to activin, consistent with the low amounts of this potent factor that are necessary to modulate cellular responses. BioEssays 22:689–696, 2000. © 2000 John Wiley & Sons, Inc.