High impact information on Klp64D

• Immunostaining for KLP68D and ribonucleic acid in situ hybridization for KLP64D demonstrated their preferential expression in cholinergic neurons [1].
• Soluble KIF2 exists without a light chain, and KIF2's associated-vesicles, immunoprecipitated by anti-KIF2 antibody, are different from those carried by existing motors such as kinesin and KIF3A [2].
• All these defects are rescued by exclusive expression of DmKAP and KLP64D/KIF3A in the JO neurons of respective mutants [3].
• Quantification analysis further showed that mutations in Klp64D could independently affect the anterograde transport of AChE even before that of ChAT [4].
• Mutations in the kinesin-2 motor subunit Klp64D and separate siRNA-mediated knock-outs of all the three kinesin-2 subunits disrupt the ChAT and AChE transports, and these antigens accumulate in discrete nonoverlapping punctae in neuronal cell bodies and axons [4].

Anatomical context of Klp64D

• Drosophila KAP interacts with the kinesin II motor subunit KLP64D to assemble chordotonal sensory cilia, but not sperm tails [3].

Other interactions of Klp64D

• Mutations in Klp64D, which codes for a Kinesin II motor subunit in Drosophila, show similar ciliary defects [3].

References