Comments on “Structural basis for microtubule binding and release by dynein”.

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.

 

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2 thoughts on “Comments on “Structural basis for microtubule binding and release by dynein”.

  1. Any thoughts on how the cell might tune the dynamic salt bridge, other than local changes in ionic strength (which seems unlikely)?

  2. Thanks for the comment Dynein Dude.
    Perhaps this salt bridge doesn’t need to be regulated. Could one have a situation where the salt bridge provides the enhanced dynamic range and then processivity (or other features) are modulated by association of accessory subunits, post-translational modifications etc?
    The cell biology of the mutant incapable of forming the salt bridge could be an interesting one to look at.

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