| First Author | Albracht CD | Year | 2016 |
| Journal | J Biol Chem | Volume | 291 |
| Issue | 44 | Pages | 23248-23256 |
| PubMed ID | 27637334 | Mgi Jnum | J:237348 |
| Mgi Id | MGI:5812602 | Doi | 10.1074/jbc.M116.752196 |
| Citation | Albracht CD, et al. (2016) Heterodimerization of Kinesin-2 KIF3AB Modulates Entry into the Processive Run. J Biol Chem 291(44):23248-23256 |
| abstractText | Mammalian KIF3AB is an N-terminal processive kinesin-2 that is best known for its roles in intracellular transport. There has been significant interest in KIF3AB to define the key principles that underlie its processivity but also to define the mechanistic basis of its sensitivity to force. In this study, the kinetics for entry into the processive run were quantified. The results show for KIF3AB that the kinetics of microtubule association at 7 mum-1 s-1 is less than the rates observed for KIF3AA at 13 mum-1 s-1 or KIF3BB at 11.9 mum-1 s-1 ADP release after microtubule association for KIF3AB is 33 s-1 and is significantly slower than ADP release from homodimeric KIF3AA and KIF3BB, which reach 80-90 s-1 To explore the interhead communication implied by the rate differences at these first steps, we compared the kinetics of KIF3AB microtubule association followed by ADP release with the kinetics for mixtures of KIF3AA plus KIF3BB. Surprisingly, the kinetics of KIF3AB are not equivalent to any of the mixtures of KIF3AA + KIF3BB. In fact, the transients for each of the mixtures overlay the transients for KIF3AA and KIF3BB. These results reveal that intermolecular communication within the KIF3AB heterodimer modulates entry into the processive run, and the results suggest that it is the high rate of microtubule association that drives rebinding to the microtubule after force-dependent motor detachment. |
