Disease relevance of Klp68D

• KLP68D protein produced in Escherichia coli is, like kinesin itself, a plus-end directed microtubule motor [1].

High impact information on Klp68D

• Immunostaining for KLP68D and ribonucleic acid in situ hybridization for KLP64D demonstrated their preferential expression in cholinergic neurons [2].
• KLP68D was also found to accumulate in cholinergic neurons in axonal obstructions caused by the loss of kinesin light chain [2].
• Together, these data suggest that kinesin-II is required for the axonal transport of a soluble enzyme, choline acetyltransferase, in a specific subset of neurons in Drosophila [2].
• Thus, KLP68D may be used for anterograde axonal transport and could conceivably move cargoes in fly neurons different than those moved by kinesin heavy chain or other plus-end directed motors [1].
• This paper describes the molecular and biochemical properties of KLP68D, a new kinesin-like motor protein in Drosophila melanogaster [1].

Biological context of Klp68D

• In situ hybridization analysis of KLP68D RNA in Drosophila embryos indicates that the KLP68D gene is expressed primarily in the central nervous system and in a subset of the peripheral nervous system during embryogenesis [1].
• Follicle separation during Drosophila oogenesis requires the activity of the kinesin II-associated polypeptide Kap in germline cells [3].

Anatomical context of Klp68D

• BACKGROUND: Kinesin II-mediated anterograde intraflagellar transport (IFT) is essential for the assembly and maintenance of flagella and cilia in various cell types [4].
• However, the flagellar assembly in Drosophila spermatids does not require Kinesin II and is independent of IFT [4].
• CONCLUSIONS: KAP plays an essential role in Kinesin II function, which is required for the axoneme growth and maintenance of the cilia in Drosophila type I sensory neurons [4].
• Drosophila KAP interacts with the kinesin II motor subunit KLP64D to assemble chordotonal sensory cilia, but not sperm tails [4].

Physical interactions of Klp68D

• Drosophila Kinesin II was shown to be essential for the axonal transport of choline acetyltransferase in a specific set of neurons [3].

Other interactions of Klp68D

• The DmKAP expression pattern in the nervous system corresponds well with that of Klp64D and Klp68D as reported earlier [5].
• Sequence analysis of a full-length cDNA encoding KLP68D demonstrates that this protein has a domain that shares significant sequence identity with the entire 340-amin acid kinesin heavy chain motor domain [1].

References