Disease relevance of KIF1C

• Finally, the susceptibility of certain inbred mice to anthrax lethal toxin was associated with mutations in the kinesin-like protein Kif1C, a discovery that could help to explain how anthrax toxin kills animals [1].

High impact information on KIF1C

• The kinesin KIF1C and microtubule plus ends regulate podosome dynamics in macrophages [2].
• KIF1C, a recently identified member of the KIF1/Unc104 family, was shown to be involved in the retrograde vesicle transport from the Golgi-apparatus to the endoplasmic reticulum [3].
• Serine 1092 was a substrate for the protein kinase casein kinase II in vitro, and inhibition of casein kinase II in cells diminished the association of KIF1C with 14-3-3gamma [3].
• This brefeldin A-induced flow of Golgi membranes into the ER was inhibited in cells transiently overexpressing catalytically inactive KIF1C [4].
• Interestingly, KIF1C was tyrosine-phosphorylated after peroxovanadate stimulation when overexpressed in 293 or NIH3T3 fibroblasts or in native C2C12 cells [4].

Anatomical context of KIF1C

• Like its homologues, the 1103-amino acid protein KIF1C consists of an amino-terminal motor domain followed by a U104 domain and probably binds to target membranes through carboxyl-terminal sequences [4].
• BACKGROUND: Members of the Kinesin-3 family of kinesin-like proteins mediate transport of axonal vesicles (KIF1A, KIF1Bbeta), distribution of mitochondria (KIF1Balpha) and anterograde Golgi to ER vesicle transport (KIF1C) [5].

Analytical, diagnostic and therapeutic context of KIF1C

• Using immunofluorescence, we found that KIF1C is localized primarily at the Golgi apparatus [4].

References