Nov 23, 2006

A role for kinesin-2 in COPI-dependent recycling between the ER and the Golgi complex

Current Biology : CB
Tobias StauberIsabelle Vernos


Transport carriers operating between early compartments in the mammalian secretory pathway have to travel long distances in the cell by mostly relying on the microtubule network and its associated motor proteins. Although anterograde transport from the endoplasmic reticulum (ER) to the Golgi complex is mediated by cytoplasmic dynein, the identity of the motor(s) mediating transport in the retrograde direction is presently unclear. Some studies have suggested that the heterotrimeric kinesin-2 complex plays a role in transport between the ER and the Golgi. Here, we have examined kinesin-2 function by using an RNA-interference approach to downregulate the expression of KAP3, the nonmotor subunit of kinesin-2, in HeLa cells. KAP3 silencing results in the fragmentation of the Golgi apparatus and a change in the steady-state localization of the KDEL-receptor (KDEL-R). Using specific transport assays, we show that the rate of anterograde secretory traffic is unaffected in these cells but that KDEL-R-dependent retrograde transport is strongly abrogated. Our data strongly support a role for kinesin-2 in the KDEL-R-/COPI-dependent retrograde transport pathway from the Golgi complex to the ER.

Mentioned in this Paper

Establishment and Maintenance of Localization
Immunofluorescence Assay
Biochemical Pathway
Dynein Activity
Tissue Membrane
KIFAP3 protein, human
RAB6A gene
Coat Protein Complex I
Abnormal Fragmented Structure

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