IFT27 links the BBSome to IFT for maintenance of the ciliary signaling compartment.

Vertebrate hedgehog signaling is coordinated by the differential localization of the receptors patched-1 and Smoothened in the primary cilium. Cilia assembly is mediated by intraflagellar transport (IFT), and cilia defects disrupt hedgehog signaling, causing many structural birth defects. We generated Ift25 and Ift27 knockout mice and show that they have structural birth defects indicative of hedgehog signaling dysfunction.

Distinct functions for IFT140 and IFT20 in opsin transport.

In the vertebrate retina, light is detected by the outer segments of photoreceptor rods and cones, which are highly modified cilia. Like other cilia, outer segments have no protein synthetic capacity and depend on proteins made in the cell body for their formation and maintenance. The mechanism of transport into the outer segment is not fully understood but intraflagellar transport (IFT) is thought to be a major mechanism for moving protein from the cell body into the cilium.

IFT25 links the signal-dependent movement of Hedgehog components to intraflagellar transport.

The intraflagellar transport (IFT) system is required for building primary cilia, sensory organelles that cells use to respond to their environment. IFT particles are composed of about 20 proteins, and these proteins are highly conserved across ciliated species. IFT25, however, is absent from some ciliated organisms, suggesting that it may have a unique role distinct from ciliogenesis.

Trait empathy as a predictor of individual differences in perceived loneliness.

Loneliness has been shown to be inversely correlated with empathy in younger adults. The present study extends previous research by investigating the association between empathy and loneliness across the adult lifespan and examining the role of relevant demographic and personality factors. 110 community-dwelling adults (18 to 81 years old) completed the UCLA Loneliness Scale and the Empathy Quotient.

IFT20 is required for opsin trafficking and photoreceptor outer segment development.

The light-detecting outer segments of vertebrate photoreceptors are cilia. Like other cilia, all materials needed for assembly and maintenance are synthesized in the cell body and transported into the cilium. The highly elaborated nature of the outer segment and its high rate of turnover necessitate unusually high levels of transport into the cilium.

Characterization of mouse IFT complex B.

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.

MAPK interacts with XGef and is required for CPEB activation during meiosis in Xenopus oocytes.

Meiotic progression in Xenopus oocytes, and all other oocytes investigated, is dependent on polyadenylation-induced translation of stockpiled maternal mRNAs. Early during meiotic resumption, phosphorylation of CPE-binding protein (CPEB) is required for polyadenylation-induced translation of mRNAs encoding cell cycle regulators. Xenopus Gef (XGef), a Rho-family guanine-exchange factor, influences the activating phosphorylation of CPEB.

XGef is a CPEB-interacting protein involved in Xenopus oocyte maturation.

XGef was isolated in a screen for proteins interacting with CPEB, a regulator of mRNA translation in early Xenopus development. XGef is a Rho-family guanine nucleotide exchange factor and activates Cdc42 in mammalian cells. Endogenous XGef (58 kDa) interacts with recombinant CPEB, and recombinant XGef interacts with endogenous CPEB in Xenopus oocytes.

Differential processing of the Xenopus ATP(CTP):tRNA nucleotidyltransferase mRNA.

The ATP(CTP):tRNA nucleotidyltransferase (CCA-adding enzyme) adds CCA to the 3(') end of immature or damaged tRNAs. It is reported on here the cloning, expression analysis, and functional characterization of the Xenopus CCA-adding enzyme, XCCA (GenBank Accession #AF466151). It is demonstrated that XCCA adds cytosine and adenosine residues to the ends of prepared tRNA and is therefore a functional CCA-adding enzyme.