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Biomedical subjects

Pierre Pontarotti

Publications and source records attributed to Pierre Pontarotti.

21 records · Page 2Linked to original sources

Cutting edge: recruitment of the ancestral fyn gene during emergence of the adaptive immune system.

The adaptive immune system (AIS) is characterized by the MHC molecules and the rearranging Ag receptors, and was established in a common ancestor of jawed vertebrates. Fyn, a Src-family tyrosine kinases, is important for normal development and function of T lymphocytes and neuronal cells. Indeed, as the result of an alternative splicing of a distinct exon 7, fyn encodes for two isoforms, FynT in T lymphocytes and FynB in the brain. How this alternative splicing of fyn transcripts has emerged and evolved in relation to the setting of the AIS remains to be established. In this study, we show that exon capture in a vertebrate ancestor by the fynT-like gene has yielded a novel fyn-encoded isoform, fynB. Unexpectedly, the newly established AIS recruited the ancestral Fyn isoform, FynT, whereas the CNS expresses the most recent one, FynB. These results shed new light on the emergence of the AIS.

Adaptation, Physiological↗

The LAP family: a phylogenetic point of view.

Recently, the LAP (for 'LRR and PDZ') family of adaptor proteins was described in vertebrates and invertebrates. The proteins are involved in cell polarity and receptor targeting, and they contain both LRR and PDZ domains in the same molecule, a combination that is specifically bilaterian. A search of available genome sequences reveals a limited number of lap genes, which we have classified by phylogenetic analysis. We propose a functional hypothesis for the origin of this protein family in bilaterians, and give a phylogenetic interpretation of their diversity.

Amino Acid Sequence↗

Leukocyte Ig-like receptor complex (LRC) in mice and men.

Here, we compare the architecture of membrane receptors with extracellular Ig-like domains located within the leukocyte Ig-like receptor complex (LRC) of humans and mice. The receptors can be classified broadly into four groups, based on the homology of their Ig-like domains and gene architecture. Receptors in the first group are characterized by the presence of the Ig constant type 2-1 (IgC2-1) and variant Ig (vlg) domains, and include the leukocyte Ig-like receptors (LILRs) and murine paired Ig-activating receptors (PIRs). The second group of receptors possess an IgC2-2 domain and comprise the killer-cell Ig-like receptors (KIRs) and platelet collagen receptor glycoprotein VI (GPVI). The third group consists of receptors with IgC2-1, and IgC2-3 or IgC2-4 domains, and includes the receptor for IgA Fc (FCAR), NKp46 and murine Ly94. The fourth group, with a single extracellular IgC2-1 domain, consists of the leukocyte-associated Ig-like receptors (LAIRs). The genomic organization of and evolutionary associations between these receptors and their domains are examined.

Animals↗