Photoreceptor IFT complexes containing chaperones, guanylyl cyclase 1 and rhodopsin. Traffic 2009 Jun;10(6):648-63
Date
03/24/2009Pubmed ID
19302411Pubmed Central ID
PMC2827254DOI
10.1111/j.1600-0854.2009.00896.xScopus ID
2-s2.0-65749105231 (requires institutional sign-in at Scopus site) 57 CitationsAbstract
Intraflagellar transport (IFT) provides a mechanism for the transport of cilium-specific proteins, but the mechanisms for linkage of cargo and IFT proteins have not been identified. Using the sensory outer segments (OS) of photoreceptors, which are derived from sensory cilia, we have identified IFT-cargo complexes containing IFT proteins, kinesin 2 family proteins, two photoreceptor-specific membrane proteins, guanylyl cyclase 1 (GC1, Gucy2e) and rhodopsin (RHO), and the chaperones, mammalian relative of DNAJ, DnajB6 (MRJ), and HSC70 (Hspa8). Analysis of these complexes leads to a model in which MRJ through its binding to IFT88 and GC1 plays a critical role in formation or stabilization of the IFT-cargo complexes. Consistent with the function of MRJ in the activation of HSC70 ATPase activity, Mg-ATP enhances the co-IP of GC1, RHO, and MRJ with IFT proteins. Furthermore, RNAi knockdown of MRJ in IMCD3 cells expressing GC1-green fluorescent protein (GFP) reduces cilium membrane targeting of GC1-GFP without apparent effect on cilium elongation.
Author List
Bhowmick R, Li M, Sun J, Baker SA, Insinna C, Besharse JCMESH terms used to index this publication - Major topics in bold
Amino Acid SequenceAnimals
Guanylate Cyclase
Immunohistochemistry
Mice
Molecular Chaperones
Molecular Sequence Data
Photoreceptor Cells, Vertebrate
Rhodopsin
Two-Hybrid System Techniques