UMMS Affiliation

Program in Molecular Medicine; Department of Physiology

Publication Date

12-30-2008

Document Type

Article

Subjects

Animals; Binding Sites; Carrier Proteins; Cell Line; Cells, Cultured; Cilia; Golgi Apparatus; Mice; Mice, Inbred C57BL; Mice, Knockout; Mice, Transgenic; Nuclear Proteins; Protein Binding; Protein Transport

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

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.

Rights and Permissions

Citation: PLoS Genet. 2008 Dec;4(12):e1000315. Epub 2008 Dec 26. Link to article on publisher's site

DOI of Published Version

10.1371/journal.pgen.1000315

Related Resources

Link to Article in PubMed

Journal/Book/Conference Title

PLoS genetics

PubMed ID

19112494

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