Title

Characterization of mouse IFT complex B

PubMed ID

19253336

UMMS Affiliation

Program in Molecular Medicine

Date

3-3-2009

Document Type

Article

Subjects

Animals; Blotting, Western; Carrier Proteins; Cell Line; Cilia; Flagella; Golgi Apparatus; Immunoprecipitation; Intracellular Signaling Peptides and Proteins; Mice; Nuclear Proteins; Protein Binding; Tumor Suppressor Proteins

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

The primary cilium plays a key role in the development of mammals and in the maintenance of health. Primary cilia are assembled and maintained by the process of intraflagellar transport (IFT). In this work, we characterize mouse IFT complex B by identifying all of the mammalian orthologues of complex B and B-associated proteins previously identified in Chlamydomonas and Caenorhabditis and also identify a new component (IFT25/Hspb11) of complex B by database analysis. We tagged each of these proteins with the FLAG epitope and show that all except IFT172 and IFT20 localize to cilia and the peri-basal body or centrosomal region at the base of cilia. All of the proteins except IFT172 immunoprecipitate IFT88 indicating that they are co-assembled into a complex. IFT20 is the only complex B protein that localizes to the Golgi apparatus. However, overexpression of IFT54/Traf3ip1, the mouse orthologue of Dyf-11/Elipsa, displaces IFT20 from the Golgi apparatus. IFT54 does not localize to the Golgi complex nor does it interact with GMAP210, which is the protein that anchors IFT20 to the Golgi apparatus. This suggests that IFT54s effect on IFT20 is a dominant negative phenotype caused by its overexpression. Cell Motil. Cytoskeleton 2009. (c) 2009 Wiley-Liss, Inc.

Rights and Permissions

Citation: Cell Motil Cytoskeleton. 2009 Aug;66(8):457-68. Link to article on publisher's site

Related Resources

Link to Article in PubMed