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Publication Abstract from PubMed

Processive kinesin motors often contain a coiled-coil neck that controls the directionality and processivity. However, the neck coil (NC) of kinesin-3 is too short to form a stable coiled-coil dimer. Here, we found that the CC1-FHA tandem (that is connected to NC by P390) of kinesin-3 KIF13A assembles as an extended dimer. With the removal of P390, the NC-CC1 tandem of KIF13A unexpectedly forms a continuous coiled-coil dimer that can be well aligned into the CC1-FHA dimer. The reverse introduction of P390 breaks the NC-CC1 coiled-coil dimer but provides the intrinsic flexibility to couple NC with the CC1-FHA tandem. Mutations of either NC, CC1 or the FHA domain all significantly impaired the motor activity. Thus, the three elements within the NC-CC1-FHA tandem of KIF13A are structurally interrelated to form a stable dimer for activating the motor. This work also provides the first direct structural evidence to support the formation of a coiled-coil neck by the short characteristic neck domain of kinesin-3.

Structural correlation of the neck coil with the CC1-FHA tandem for active kinesin-3 KIF13A.,Ren J, Huo L, Wang W, Zhang Y, Li W, Lou J, Xu T, Feng W J Biol Chem. 2015 Dec 17. pii: jbc.M115.689091. PMID:26680000^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.