View source for PILRB

{{Short description|Protein-coding gene in the species Homo sapiens}}
{{Infobox_gene}}
'''Paired immunoglobulin-like type 2 receptor beta''' is a [[protein]] that in humans is encoded by the '''''PILRB''''' [[gene]].<ref name="pmid10660620">{{cite journal | vauthors = Mousseau DD, Banville D, L'Abbé D, Bouchard P, Shen SH | title = PILRalpha, a novel immunoreceptor tyrosine-based inhibitory motif-bearing protein, recruits SHP-1 upon tyrosine phosphorylation and is paired with the truncated counterpart PILRbeta | journal = The Journal of Biological Chemistry | volume = 275 | issue = 6 | pages = 4467–74 | date = February 2000 | pmid = 10660620 | doi = 10.1074/jbc.275.6.4467 | doi-access = free | url = https://www.openaccessrepository.it/record/94145/files/fulltext.pdf }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PILRB paired immunoglobin-like type 2 receptor beta| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29990}}</ref>
== Function ==
[[Cell signaling]] pathways rely on a dynamic interaction between activating and inhibiting processes. [[PTPN6|SHP-1]]-mediated [[dephosphorylation]] of protein [[tyrosine]] residues is central to the regulation of several cell signaling pathways. Two types of inhibitory receptor superfamily members are [[immunoreceptor tyrosine-based inhibitory motif]] (ITIM)-bearing receptors and their non-ITIM-bearing, activating counterparts.
Control of cell signaling via SHP-1 is thought to occur through a balance between [[PILRA|PILRalpha]]-mediated inhibition and PILRbeta-mediated activation. These paired [[immunoglobulin]]-like receptor genes are located in a tandem head-to-tail orientation on [[chromosome 7]]. This particular gene encodes the non-ITIM-bearing member of the receptor pair, which has a truncated [[cytoplasmic]] tail relative to its ITIM-bearing partner and functions in the activating role. [[Alternative splicing]] has been observed at this locus and three variants, encoding two distinct isoforms, are described. Additional transcript variants have been identified but their full-length nature has not been determined.<ref name="entrez" />
The mouse [[homolog]] of PILRbeta has been studied in mice and found to have one known natural ligand, [[CD99]], though it is unclear if this interaction occurs in the human homologs.<ref name="lu_2014">{{cite journal | vauthors = Lu Q, Lu G, Qi J, Wang H, Xuan Y, Wang Q, Li Y, Zhang Y, Zheng C, Fan Z, Yan J, Gao GF | display-authors = 6 | title = PILRα and PILRβ have a siglec fold and provide the basis of binding to sialic acid | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 111 | issue = 22 | pages = 8221–6 | date = June 2014 | pmid = 24843130 | doi = 10.1073/pnas.1320716111 | pmc = 4050567 | bibcode = 2014PNAS..111.8221L | doi-access = free }}</ref>
== Structure ==
As with other [[paired receptors]], PILRbeta has a truncated [[cytoplasmic]] tail compared to PILRalpha and features a charged residue within its [[transmembrane domain]].<ref name="mousseau_2000">{{cite journal | vauthors = Mousseau DD, Banville D, L'Abbé D, Bouchard P, Shen SH | title = PILRalpha, a novel immunoreceptor tyrosine-based inhibitory motif-bearing protein, recruits SHP-1 upon tyrosine phosphorylation and is paired with the truncated counterpart PILRbeta | journal = The Journal of Biological Chemistry | volume = 275 | issue = 6 | pages = 4467–74 | date = February 2000 | pmid = 10660620 | doi = 10.1074/jbc.275.6.4467 | doi-access = free | url = https://www.openaccessrepository.it/record/94145/files/fulltext.pdf }}</ref><ref name="wilson_2006">{{cite journal | vauthors = Wilson MD, Cheung J, Martindale DW, Scherer SW, Koop BF | title = Comparative analysis of the paired immunoglobulin-like receptor (PILR) locus in six mammalian genomes: duplication, conversion, and the birth of new genes | journal = Physiological Genomics | volume = 27 | issue = 3 | pages = 201–18 | date = November 2006 | pmid = 16926269 | doi = 10.1152/physiolgenomics.00284.2005 }}</ref> PILRbeta has an extracellular [[protein domain|domain]] with a [[siglec]]-like [[immunoglobulin]] [[protein fold|fold]] that substitutes [[hydrophobic]] interactions for the siglec fold's characteristic [[disulfide bond]]. The structure of this domain is very similar to that of PILRalpha, but the two proteins nevertheless have different [[binding affinities]] for [[sialic acid]].<ref name="lu_2014" />
== References ==
{{reflist|2}}
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