The Golgin GMAP210/TRIP11 anchors IFT20 to the Golgi complex

Eukaryotic cells often use proteins localized to the ciliary membrane to monitor the extracellular environment. The mechanism by which proteins are sorted, specifically to this subdomain of the plasma membrane, is almost completely unknown. Previously, we showed that the IFT20 subunit of the intrafl...

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Bibliographic Details
Published in:PLoS genetics 2008-12, Vol.4 (12), p.e1000315-e1000315
Main Authors: Follit, John A, San Agustin, Jovenal T, Xu, Fenghui, Jonassen, Julie A, Samtani, Rajeev, Lo, Cecilia W, Pazour, Gregory J
Format: Article
Language:English
Subjects:
Animals
Binding Sites
Carrier Proteins - chemistry
Carrier Proteins - genetics
Carrier Proteins - metabolism
Cell Biology
Cell Line
Cells, Cultured
Cilia - metabolism
Cytoskeletal Proteins
Defects
Disease
Genetics and Genomics
Genetics and Genomics/Disease Models
Golgi Apparatus - chemistry
Golgi Apparatus - genetics
Golgi Apparatus - metabolism
Heart
Mice
Mice, Inbred C57BL
Mice, Knockout
Mice, Transgenic
Nuclear Proteins - chemistry
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
Plasma
Protein Binding
Protein Transport
Proteins
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Summary:Eukaryotic cells often use proteins localized to the ciliary membrane to monitor the extracellular environment. The mechanism by which proteins are sorted, specifically to this subdomain of the plasma membrane, is almost completely unknown. Previously, we showed that the IFT20 subunit of the intraflagellar transport particle is localized to the Golgi complex, in addition to the cilium and centrosome, and hypothesized that the Golgi pool of IFT20 plays a role in sorting proteins to the ciliary membrane. Here, we show that IFT20 is anchored to the Golgi complex by the golgin protein GMAP210/Trip11. Mice lacking GMAP210 die at birth with a pleiotropic phenotype that includes growth restriction, ventricular septal defects of the heart, omphalocele, and lung hypoplasia. Cells lacking GMAP210 have normal Golgi structure, but IFT20 is no longer localized to this organelle. GMAP210 is not absolutely required for ciliary assembly, but cilia on GMAP210 mutant cells are shorter than normal and have reduced amounts of the membrane protein polycystin-2 localized to them. This work suggests that GMAP210 and IFT20 function together at the Golgi in the sorting or transport of proteins destined for the ciliary membrane.
ISSN:1553-7404
1553-7390
1553-7404
DOI:10.1371/journal.pgen.1000315