Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 38, Issue 11, Pages 538-545Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2013.08.005
Keywords
sensor domains; output domains; signal transduction
Categories
Funding
- Collaborative Research Centre [766]
- Deutsche Forschungsgemeinschaft [B8]
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Modular proteins possess N-terminal sensor domains connected with different C-terminal output domains. Different output domains, for example, phosphodiesterases adenylyl cyclases, are regulated by identical N-terminal domains. Therefore, the mechanisms of intraprotein signaling share properties suitable to regulation of disparate output enzymes, which see the same signal but react differently. The common denominator is a reversible switch of folding/unfolding that connects sensor and output domains. In the inhibited state, output domains are restrained, whereas in the activated state domains are released to assemble according to intrinsic domain properties. We review recent work investigating the mechanism of intraprotein signaling and discuss how this signaling mechanism may have contributed to the evolutionary diversity of specific small molecule-binding domains without loss of regulatory properties.
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