The lipid binding pleckstrin homology domain in UNC-104 kinesin is necessary for synaptic vesicle transport in Caenorhabditis elegans.

By Dieter R. Klopfenstein, R. Vale. 2004

158 citations recorded by the source corpus.

Subfields: Aging, Cell Biology

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In Cell Biology

1. Yosuke Tanaka
2. Shinsuke Niwa
3. Alison E. Twelvetrees
4. E. Holzbaur
5. N. Hirokawa
6. Debashish Chowdhury

Citations in the corpus

• Kinesin superfamily motor proteins and intracellular transport (2009, background): “, and the pleckstrin homology (PH) domain of KIF1A and KIF1Bβ is necessary, but not sufficient, to transport cargo to axon terminal”
• Molecular motors in neurons: transport mechanisms and roles in brain function, development, and disease. (2010, unknown): “It has been suggested that the PH domain is required but not sufficient for cargo transport (Klopfenstein et al., 2002; Klopfenstein and Vale, 2004).”
• AXONAL TRANSPORT: CARGO-SPECIFIC MECHANISMS OF MOTILITY AND REGULATION (2014, background): “Kinesin-3 motors undergo cargo-mediated dimerization, which leads to the formation of highly processive anterograde motors to drive efficient delivery of synaptic components (Klopfenstein and Vale, 2004; Soppina et al., 2014).”