The phylogenetic position of the Dura Language of Nepal

The precise phylogenetic propinquity of Dura within the Tibeto-Burman or Trans-Himalayan language family has hitherto been indeterminate. In the absence of compelling comparative evidence, the language has previously been assigned to a subgroup in its own right within the linguistic phylum as a whole. Meanwhile, the Dura language is effectively extinct, although attempts at revival may be undertaken by well-intentioned members of Dura ethnicity. On the basis of a comprehensive study and analysis of all of the extant Dura language material, the phylogenetic position of the language within the family will be clarified. Comparative evidence from the Dura lexicon, its nominal and verbal morphology as well as from syntactic and phonological properties is adduced to determine the phylogenetic position of Dura. Moreover, this result will help explain some of the sociocultural realities associated with the Dura language community in Lamjung, Nepal

Phylogenetic analysis of receptor FgfrL1 shows divergence of the C-terminal end in rodents

FGFRL1 is a member of the fibroblast growth factor receptor (FGFR) family. Similar to the classical receptors FGFR1-FGFR4, it contains three extracellular Ig-like domains and a single transmembrane domain. However, it lacks the intracellular tyrosine kinase domain that would be required for signal transduction, but instead contains a short intracellular tail with a peculiar histidine-rich motif. This motif has been conserved during evolution from mollusks to echinoderms and vertebrates. Only the sequences of FgfrL1 from a few rodents diverge at the C-terminal region from the canonical sequence, as they appear to have suffered a frameshift mutation within the histidine-rich motif. This mutation is observed in mouse, rat and hamster, but not in the closely related rodents mole rat (Nannospalax) and jerboa (Jaculus), suggesting that it has occurred after branching of the Muridae and Cricetidae from the Dipodidae and Spalacidae. The consequence of the frameshift is a deletion of a few histidine residues and an extension of the C-terminus by about 40 unrelated amino acids. A similar frameshift mutation has also been observed in a human patient with a craniosynostosis syndrome as well as in several patients with colorectal cancer and bladder tumors, suggesting that the histidine-rich motif is prone to mutation. The reason why this motif was conserved during evolution in most species, but not in mice, is not clear.