Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.6.4.4 (kinesin)
 5,033 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

KIF1Bbeta is a member of the Kinesin superfamily proteins (KIFs), which are microtubule-dependent molecular motors that are involved in various intracellular organellar transport processes. KIF1Bbeta is not restricted to neuronal systems, however, is widely expressed in other tissues, even though the function of KIF1Bbeta is still unclear. To elucidate the KIF1Bbeta-binding proteins in non-neuronal cells, we used the yeast two-hybrid system, and found a specific interaction of KIF1Bbeta and the sorting nexin (SNX) 17. The C-terminal region of SNX17 is required for the binding with KIF1Bbeta. SNX17 protein bound to the specific region of KIF1Bbeta (813-916. aa), but not to other kinesin family members. In addition, this specific interaction was also observed in the Glutathione S-transferase pull-down assay. An antibody to SNX17 specifically co-immunoprecipitated KIF1Bbeta associated with SNX17 from mouse brain extracts. These results suggest that SNX17 might be involved in the KIF1Bbeta-mediated transport as a KIF1Bbeta adaptor protein.
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PMID:Sorting Nexin 17 Interacts Directly with Kinesin Superfamily KIF1Bbeta Protein. 1996 56

We recently demonstrated that dynein and kinesin motors drive multiple aspects of endosomal function in mammalian cells. These functions include driving motility, maintaining morphology (notably through providing longitudinal tension to support vesicle fission), and driving cargo sorting. Microtubule motors drive bidirectional motility during traffic between the endoplasmic reticulum (ER) and Golgi. Here, we have examined the role of microtubule motors in transport carrier motility, morphology, and domain organization during ER-to-Golgi transport. We show that, consistent with our findings for endosomal dynamics, microtubule motor function during ER-to-Golgi transport of secretory cargo is required for motility, morphology, and cargo sorting within vesicular tubular carriers en route to the Golgi. Our data are consistent with previous findings that defined roles for dynein-1, kinesin-1 (KIF5B) and kinesin-2 in this trafficking step. Our high resolution tracking data identify some intriguing aspects. Depletion of kinesin-1 reduces the number of motile structures seen, which is in line with other findings relating to the role of kinesin-1 in ER export. However, those transport carriers that were produced had a much greater run length suggesting that this motor can act as a brake on anterograde motility. Kinesin-2 depletion did not significantly reduce the number of motile transport carriers but did cause a similar increase in run length. These data suggest that kinesins act as negative regulators of ER-to-Golgi transport. Depletion of dynein not only reduced the number of motile carriers formed but also caused tubulation of carriers similar to that seen for sorting nexin-coated early endosomes. Our data indicated that the previously observed anterograde-retrograde polarity of transport carriers in transit to the Golgi from the ER is maintained by microtubule motor function.
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PMID:Opposing microtubule motors control motility, morphology and cargo segregation during ER-to-Golgi transport. 2470 13