Export of membrane proteins from the Golgi complex to the primary cilium requires the kinesin motor, KIFC1

Microtubule‐based motors contribute to the efficiency and selectivity of Golgi exit and post‐Golgi transport of membrane proteins that are targeted to distinct compartments. Cytoplasmic dynein moves post‐Golgi vesicles that carry rhodopsin toward the base of the connecting cilium in photoreceptor ce...

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Published in:	The FASEB journal Vol. 32; no. 2; pp. 957 - 968
Main Authors:	Lee, Si‐Hyung, Too, Kwangsic, Jung, Eun Ji, Hong, Hyowon, Seo, Jimyung, Kim, Joon
Format:	Journal Article
Language:	English
Published:	United States Federation of American Societies for Experimental Biology 01-02-2018
Subjects:	Adaptor Proteins, Signal Transducing - genetics Adaptor Proteins, Signal Transducing - metabolism ASAP1 Carrier Proteins - genetics Carrier Proteins - metabolism Cell Line Cilia - genetics Cilia - metabolism ciliogenesis Cytoskeletal Proteins dynein Golgi Apparatus - genetics Golgi Apparatus - metabolism Kinesin - genetics Kinesin - metabolism Membrane Proteins - genetics Membrane Proteins - metabolism Nuclear Proteins - genetics Nuclear Proteins - metabolism Protein Transport - physiology TTBK2 dynein ASAP1 ciliogenesis TTBK2
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Summary:	Microtubule‐based motors contribute to the efficiency and selectivity of Golgi exit and post‐Golgi transport of membrane proteins that are targeted to distinct compartments. Cytoplasmic dynein moves post‐Golgi vesicles that carry rhodopsin toward the base of the connecting cilium in photoreceptor cells; however, the identity of the motors that are involved in the vesicular trafficking of ciliary membrane proteins in nonphotoreceptor cells remains unclear. Here, we demonstrate that the minus end–directed kinesin KIFC1 (kinesin family member C1) is required for both ciliary membrane protein transport and serum starvation–induced ciliogenesis in retinal pigmented epithelial 1 cells. Although KIFC1 is known as a mitotic motor that is sequestered in the nucleus during interphase, KIFC1 immunoreactivity appeared in the Golgi region after serum starvation. Knockdown of KIFC1 inhibited the export of ciliary receptors from the Golgi complex. KIFC1 overexpression affected the Golgi localization of GMAP210 (Golgi microtubule‐associated protein 210) and IFT20 (intraflagellar transport 20), which are involved in membrane protein transport to cilia. Moreover, KIFC1 physically interacted with ASAP1 (ADP‐ribosylation factor GTPase‐activating protein with SH3 domain, ankyrin repeat and PH domain 1), which regulates the budding of rhodopsin transport carriers from the Golgi complex, and KIFC1 depletion caused Golgi accumulation of ASAP1. A decrease in the centrosomal levels of IFT20 and TTBK2 (τ‐tubulin kinase 2) was associated with ciliogenesis defects in KIFC1‐depleted cells. Our results suggest that KIFC1 plays roles in the Golgi exit of ciliary receptors and in the recruitment of ciliogenesis regulators.—Lee, S.‐H., Joo, K., Jung, E. J., Hong, H., Seo, J., Kim, J. Export of membrane proteins from the Golgi complex to the primary cilium requires the kinesin motor, KIFC1. FASEB J. 32, 957–968 (2018). www.fasebj.org
Bibliography:	These authors contributed equally to this work. ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0892-6638 1530-6860
DOI:	10.1096/fj.201700563R