Published In The Analysis Of Two Distinguished Professor Of Cell Protein Mechanisms

From the Institute of Biophysics, Chinese Academy of Sciences, the researchers at the Hong Kong University of science and technology, entitled "The CC1-FHA Tandem as a Central Hub for Controlling the Dimerization and Activation of Kinesin-3 KIF1A" article points out a CC1-FHA structure can facilitate key-driven protein-3 in series of KIF1A dimerization and activity Driving control of such proteins is presented a new law. Results published in the journal Cell Press, its Structure.

The author of the article came from Biophysics Professor xutao, respectively researcher, Hong Kong University of science and technology Professor Zhang mingjie, Feng Wei of the Institute as well as researchers, Institute belong to the same first author, Hong Kong University of science and technology and the Huazhong University of science and j.Halling (Lin Huo, transliteration), Yueyang (Yang Yue, transliteration).

Kinesin (Kinesin) is a protein Super family, is a kind of molecular motors, this protein is a polymer of the monomer composition, the "head" with ATP enzyme activity can be obtained through the hydrolysis of ATP energy, change configurations, exercise. But this protein and the dynamics of Polar Motion of microtubules protein something different, a kinesin can only be in one direction, such as kinesin-1 motion along microtubules. Main function of protein is in intracellular transport, such as pulling the chromosomes involved in mitosis, meiosis and cell migration.
Kinesin-3 KIF1A is also a member of this family, in the axonal transport and played an important role in the formation of synapses. Study shows KIF1A in vitro is single form, but in the body, but as a Dimer of continuity. Scientists know little about the dynamics of Dimer mechanism.

In order to answer this question in this article, the researchers found, connected with KIF1A CC1-FHA is a stable Dimer. Analysis of CC1-FHA structure, suggested that CC1 and the FHA connection unexpectedly is a beta-hairpin structure, this structure can integrate CC1 and FHA, assembled into an identical Dimer CC1-FHA.
More importantly, if the dissociation of the Dimer CC1-FHA, will release CC1 and beta structures, both of which are essential components of power inhibitors. Therefore, the researchers believe, CC1-FHA in-line dimmer can not only promote KIF1A Dimer formation, but also by chelating CC1/β--finger area, start the dynamic activity.

These data suggest that this CC1-FHA line structure may be regulated KIF1A dimerization, and a hub of activity, and this may also be extended to the other on the mechanism of action of kinesin-3, represents such a protein-driven control of a new law.
Kinesin, previous research has found that drive protein Kinesin carries vesicles, organelles, and other elements along the microtubule network (microtubule lattices) movement, but the movement did not seem to need the grid itself, it overturned before the Kinesin movement model is an important progress in this field.