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Biology subjects

Cavani, E.

Publications and source records attributed to Cavani, E..

2 recordsLinked to original sources

Distinct vocal flexibility encodes food identity in marmoset monkeys

Combinatorial vocal behavior, in which discrete vocal elements are recombined to expand the vocal repertoire, is a hallmark of human language and has been observed in some nonhuman primates. Here, we show that marmoset monkeys produce distinct vocalizations that discriminate food categories and items by producing long sequences dominated by a single call type whose spectral and temporal features vary. These sequences carried reliable information about food type that could be accurately predicted by trained classifiers. Moreover, rather than combining distinct call types, marmosets rely on sequencing and graded acoustic variation within a single call class to generate functionally diverse signals. These results suggest that precursors of linguistic combinatoriality and multiparameter coding are not unique to human speech but are present in nonhuman primate communication.

neuroscience↗

Missense mutations in CMS22 patients reveal that PREPL has both enzymatic and non-enzymatic functions

Congenital myasthenic syndrome-22 (CMS22) is a rare genetic disorder caused by mutations in the prolyl endopeptidase-like (PREPL) gene. Since previous reports only described patients with deletions and nonsense mutations in PREPL, nothing is known about the effect of missense mutations in the pathology of CMS22. In this study, we have characterized missense mutations in PREPL in three CMS22 patients, all with hallmark phenotypes. Biochemical evaluation revealed that these missense mutations do not impair hydrolase activity, thereby challenging the conventional diagnostic criteria. Structural analysis shows that the mutations affect regions most likely involved in intra-protein or protein-protein interactions. Indeed, binding to a selected group of known interactors was differentially reduced for the three mutants. The importance of non-hydrolytic functions of PREPL was investigated in catalytically inactive PREPL p.Ser559Ala cell lines which showed that hydrolytic activity of PREPL is needed for normal mitochondrial function but not for regulating AP1-mediated transport in the trans-Golgi network. In conclusion, these studies show that CMS22 can be caused not only by deletion and truncation of PREPL but also by missense mutations that do not necessarily result in a loss of hydrolytic activity of PREPL. Graphical abstract O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=111 SRC="FIGDIR/small/572145v1_ufig1.gif" ALT="Figure 1"> View larger version (29K): org.highwire.dtl.DTLVardef@13dc0bborg.highwire.dtl.DTLVardef@13865d6org.highwire.dtl.DTLVardef@1a5ed3borg.highwire.dtl.DTLVardef@79fdf5_HPS_FORMAT_FIGEXP M_FIG C_FIG

genetics↗