Kinesin-2 heterodimerization alters entry into a processive run along the microtubule but not stepping within the run.

ABSTRACT: Heterodimeric KIF3AC and KIF3AB, two members of the mammalian kinesin-2 family, generate force for microtubule plus end-directed cargo transport. However, the advantage of heterodimeric kinesins over homodimeric ones is not well-understood. We showed previously that microtubule association for entry into a processive run was similar in rate for KIF3AC and KIF3AB at ∼7.0 μm^-1 s^-1 Yet, for engineered homodimers of KIF3AA and KIF3BB, this constant is significantly faster at 11 μm^-1 s^-1 and much slower for KIF3CC at 2.1 μm^-1 s^-1 These results led us to hypothesize that heterodimerization of KIF3A with KIF3C and KIF3A with KIF3B altered the intrinsic catalytic properties of each motor domain. Here, we tested this hypothesis by us

SUBMITTER: Quinn SM 

PROVIDER: S-EPMC6120217 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature