The Golgin GMAP210/TRIP11 anchors IFT20 to the Golgi complex

• Published in: PLoS genetics Vol. 4; no. 12; p. e1000315
• Main Authors: Follit, John A, San Agustin, Jovenal T, Xu, Fenghui, Jonassen, Julie A, Samtani, Rajeev, Lo, Cecilia W, Pazour, Gregory J
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 01-12-2008; Public Library of Science (PLoS)
• 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
• ISSN: 1553-7404; 1553-7390; 1553-7404
• DOI: 10.1371/journal.pgen.1000315

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.