I evaluated the following article for F1000 Prime:
Redwine WB, Hernández-López R, Zou S, Huang J, Reck-Peterson SL, Leschziner AE. (2012) Structural basis for microtubule binding and release by dynein. Science 337, 1532-6. PMID: 22997337 DOI: 10.1126/science.1224151
My comments build on those from Terrence Frey (San Diego State University) which provide a nice description of the structural data in this paper.
I entirely agree with the thoughts of Terrence Frey here. The concept of a sub-maximal dynein constrained by virtue of an intramolecular salt bridge is a very intriguing one. The possibility that this provides dynein-1 with a greater “dynamic range” seems quite likely. I very much like the proposed explanation that cytoplasmic dynein-2, which is involved in long range unidirectional transport in cilia and flagella, is not constrained in this way because it lacks the possibility to form such a salt bridge. This provides a nice explanation for the need to maintain two distinct cytoplasmic dynein heavy chains.