Related to receptor tyrosine kinase
{{Short description|Protein-coding gene in the species Homo sapiens}}
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{{Infobox_gene}}
The related to receptor tyrosine kinase (RYK) gene encodes the protein Ryk.
The protein encoded by this gene is an atypical member of the family of growth factor receptor protein tyrosine kinases, differing from other members at a number of conserved residues in the activation and nucleotide binding domains. This gene product belongs to a subfamily whose members do not appear to be regulated by phosphorylation in the activation segment. It has been suggested that mediation of biological activity by recruitment of a signaling-competent auxiliary protein may occur through an as yet uncharacterized mechanism. Two alternative splice variants have been identified, encoding distinct isoforms.{{cite web|title=RYK receptor like tyrosine kinase [ Homo sapiens (human) ]|publisher=National Center for Biotechnology Information, U.S. National Library of Medicine|date=13 Mar 2020|url= https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=6259|access-date=2020-04-02}}
History
The gene encoding mouse RYK was first identified in 1992.{{cite journal|vauthors=Hovens CM, Stacker SA|title=RYK, a receptor tyrosine kinase-related molecule with unusual kinase domain motifs|journal=Proc. Natl. Acad. Sci. USA|year=1992|volume=89|issue=24|pages=11818–11822|pmid= 1334548|doi =10.1073/pnas.89.24.11818|pmc= 50648|bibcode=1992PNAS...8911818H |doi-access=free}}
Subsequently, cDNA encoding the RYK protein have been isolated from the following species.{{cite journal|vauthors=Halford MM, Stacker SA|title=Revelations of the RYK receptor|journal =BioEssays|year=2001|volume=23|issue=1|pages=34–45|pmid= 11135307|doi =10.1002/1521-1878(200101)23:1<34::AID-BIES1005>3.0.CO;2-D|s2cid=18535933 }}
Structure
In common with other receptor tyrosine kinase family members, RYK is composed of three domains, an N-terminal, extracellular ligand-binding domain, a transmembrane spanning domain and a C-terminal intracellular domain. However, in contrast to other receptor tyrosine kinases the C-terminal domain of RYK is devoid of detectable kinase activity.
Function
RYK is involved in regulation of axon growth during development of the nervous system.{{cite journal|vauthors=Hollis ER, Ishiko N, Yu T, Lu CC, Haimovich A, Tolentino K, Richman A, Tury A, Wang SH, Pessian M, Jo E, Kolodkin A, Zou Y|year=2016|title=Ryk controls remapping of motor cortex during functional recovery after spinal cord injury|journal=Nature Neuroscience|volume=19|issue=5|pages= 697–705|doi= 10.1038/nn.4282 |pmc=4847956|pmid=27065364}}
References
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Further reading
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- {{cite journal |vauthors=Partanen J, Mäkelä TP, Alitalo R, etal |title=Putative tyrosine kinases expressed in K-562 human leukemia cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 22 |pages= 8913–8917 |year= 1991 |pmid= 2247464 |doi=10.1073/pnas.87.22.8913 | pmc=55070 |doi-access=free }}
- {{cite journal |vauthors=Gough NM, Rakar S, Hovens CM, Wilks A |title=Localization of two mouse genes encoding the protein tyrosine kinase receptor-related protein RYK. |journal=Mamm. Genome |volume=6 |issue= 4 |pages= 255–6 |year= 1995 |pmid= 7613029 |doi=10.1007/BF00352411 |s2cid=2577241 }}
- {{cite journal |vauthors=Lee ST, Strunk KM, Spritz RA |title=A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes. |journal=Oncogene |volume=8 |issue= 12 |pages= 3403–3410 |year= 1993 |pmid= 8247543 }}
- {{cite journal |vauthors=Stacker SA, Hovens CM, Vitali A, etal |title=Molecular cloning and chromosomal localisation of the human homologue of a receptor related to tyrosine kinases (RYK). |journal=Oncogene |volume=8 |issue= 5 |pages= 1347–1356 |year= 1993 |pmid= 8386829 }}
- {{cite journal |vauthors=Tamagnone L, Partanen J, Armstrong E, etal |title=The human ryk cDNA sequence predicts a protein containing two putative transmembrane segments and a tyrosine kinase catalytic domain. |journal=Oncogene |volume=8 |issue= 7 |pages= 2009–2014 |year= 1993 |pmid= 8390040 }}
- {{cite journal |vauthors=Wang XC, Katso R, Butler R, etal |title=H-RYK, an unusual receptor kinase: isolation and analysis of expression in ovarian cancer. |journal=Mol. Med. |volume=2 |issue= 2 |pages= 189–203 |year= 1996 |pmid= 8726462 |doi= 10.1007/BF03401616| pmc=2230112 }}
- {{cite journal |vauthors=Katso RM, Russell RB, Ganesan TS |title=Functional analysis of H-Ryk, an atypical member of the receptor tyrosine kinase family. |journal=Mol. Cell. Biol. |volume=19 |issue= 9 |pages= 6427–6440 |year= 1999 |pmid= 10454588 |doi= 10.1128/mcb.19.9.6427| pmc=84612 }}
- {{cite journal |vauthors=Trivier E, Ganesan TS |title=RYK, a catalytically inactive receptor tyrosine kinase, associates with EphB2 and EphB3 but does not interact with AF-6. |journal=J. Biol. Chem. |volume=277 |issue= 25 |pages= 23037–43 |year= 2002 |pmid= 11956217 |doi= 10.1074/jbc.M202486200 |doi-access= free }}
- {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |bibcode=2002PNAS...9916899M |doi-access=free }}
- {{cite journal |vauthors=Brandenberger R, Wei H, Zhang S, etal |title=Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation. |journal=Nat. Biotechnol. |volume=22 |issue= 6 |pages= 707–16 |year= 2005 |pmid= 15146197 |doi= 10.1038/nbt971 |s2cid=27764390 }}
- {{cite journal |vauthors=Lu W, Yamamoto V, Ortega B, Baltimore D |title=Mammalian Ryk is a Wnt coreceptor required for stimulation of neurite outgrowth. |journal=Cell |volume=119 |issue= 1 |pages= 97–108 |year= 2004 |pmid= 15454084 |doi= 10.1016/j.cell.2004.09.019 |s2cid=18567677 |doi-access=free }}
- {{cite journal |vauthors=Watanabe A, Akita S, Tin NT, etal |title=A mutation in RYK is a genetic factor for nonsyndromic cleft lip and palate. |journal=Cleft Palate Craniofac. J. |volume=43 |issue= 3 |pages= 310–6 |year= 2006 |pmid= 16681403 |doi= 10.1597/04-145.1 |s2cid=23152169 }}
- {{cite journal |vauthors=Szafranski K, Schindler S, Taudien S, etal |title=Violating the splicing rules: TG dinucleotides function as alternative 3' splice sites in U2-dependent introns. |journal= Genome Biology|volume=8 |issue= 8 |pages= R154 |year= 2007|pmid= 17672918 |doi= 10.1186/gb-2007-8-8-r154 | pmc=2374985 |doi-access=free }}
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{{Tyrosine kinases}}
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