Related to receptor tyrosine kinase

Receptor-like tyrosine kinase
Identifiers
Symbols	RYK ; D3S3195; JTK5; JTK5A; RYK1
External IDs	OMIM: 600524 MGI: 101766 HomoloGene: 68287 IUPHAR: 1849 GeneCards: RYK Gene
EC number	2.7.10.1
Gene ontology Molecular function • protein tyrosine kinase activity • transmembrane receptor protein tyrosine kinase activity • transmembrane signaling receptor activity • protein binding • ATP binding Cellular component • nucleus • cytoplasm • plasma membrane • integral component of plasma membrane • membrane • integral component of membrane Biological process • protein phosphorylation • signal transduction • axon guidance • Wnt signaling pathway • peptidyl-tyrosine phosphorylation • corpus callosum development • neuron differentiation • neuron projection development • positive regulation of MAPK cascade Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	6259	20187
Ensembl	ENSG00000163785	ENSMUSG00000032547
UniProt	P34925	Q01887
RefSeq (mRNA)	NM_001005861	NM_001042607
RefSeq (protein)	NP_001005861	NP_001036072
Location (UCSC)	Chr 3: 134.07 – 134.25 Mb	Chr 9: 102.83 – 102.91 Mb
PubMed search

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.^[1]

History

The gene encoding mouse RYK was first identified in 1992.^[2] Subsequently cDNA encoding the RYK protein have been isolated from the following species.^[3]

• rat
• chicken
• Human
• Zebrafish
• Drosophila and
• C. elegans

Structure

In common with other receptor tyrosine kinase family members, RYK is composed of three domains, an N-terminal domain, an 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.^[3]

Function

RYK is involved in regulation of axon growth during development of the nervous system.^[4]

References

1. "Entrez Gene: RYK RYK receptor-like tyrosine kinase".
2. Hovens, CM, Stacker, SA (1992). "RYK, a receptor tyrosine kinase-related molecule with unusual kinase domain motifs". Proc. Natl. Acad. Sci. USA. 89 (24): 11818–11822. doi:10.1073/pnas.89.24.11818. PMC 50648. PMID 1334548.
3. Halford, MM, and Stacker, S.A. (2001). "Revelations of the RYK receptor". BioEssays 23 (1): 34–45. doi:10.1002/1521-1878(200101)23:1<34::AID-BIES1005>3.0.CO;2-D. PMID 11135307.
4. Edmund R Hollis, Nao Ishiko, Ting Yu, Chin-Chun Lu, Ariela Haimovich, Kristine Tolentino, Alisha Richman, Anna Tury, Shih-Hsiu Wang, Maysam Pessian, Euna Jo, Alex Kolodkin, Yimin Zou. Ryk controls remapping of motor cortex during functional recovery after spinal cord injury. Nature Neuroscience 2016; doi: 10.1038/nn.4282

Further reading

• Partanen J, Mäkelä TP, Alitalo R, et al. (1991). "Putative tyrosine kinases expressed in K-562 human leukemia cells.". Proc. Natl. Acad. Sci. U.S.A. 87 (22): 8913–8917. doi:10.1073/pnas.87.22.8913. PMC 55070. PMID 2247464.
• Gough NM, Rakar S, Hovens CM, Wilks A (1995). "Localization of two mouse genes encoding the protein tyrosine kinase receptor-related protein RYK.". Mamm. Genome 6 (4): 255–6. doi:10.1007/BF00352411. PMID 7613029.
• Lee ST, Strunk KM, Spritz RA (1993). "A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes.". Oncogene 8 (12): 3403–3410. PMID 8247543.
• Stacker SA, Hovens CM, Vitali A, et al. (1993). "Molecular cloning and chromosomal localisation of the human homologue of a receptor related to tyrosine kinases (RYK).". Oncogene 8 (5): 1347–1356. PMID 8386829.
• Tamagnone L, Partanen J, Armstrong E, et al. (1993). "The human ryk cDNA sequence predicts a protein containing two putative transmembrane segments and a tyrosine kinase catalytic domain.". Oncogene 8 (7): 2009–2014. PMID 8390040.
• Wang XC, Katso R, Butler R, et al. (1996). "H-RYK, an unusual receptor kinase: isolation and analysis of expression in ovarian cancer.". Mol. Med. 2 (2): 189–203. PMC 2230112. PMID 8726462.
• Katso RM, Russell RB, Ganesan TS (1999). "Functional analysis of H-Ryk, an atypical member of the receptor tyrosine kinase family.". Mol. Cell. Biol. 19 (9): 6427–6440. PMC 84612. PMID 10454588.
• Trivier E, Ganesan TS (2002). "RYK, a catalytically inactive receptor tyrosine kinase, associates with EphB2 and EphB3 but does not interact with AF-6.". J. Biol. Chem. 277 (25): 23037–43. doi:10.1074/jbc.M202486200. PMID 11956217.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Brandenberger R, Wei H, Zhang S, et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation.". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197.
• Lu W, Yamamoto V, Ortega B, Baltimore D (2004). "Mammalian Ryk is a Wnt coreceptor required for stimulation of neurite outgrowth.". Cell 119 (1): 97–108. doi:10.1016/j.cell.2004.09.019. PMID 15454084.
• Watanabe A, Akita S, Tin NT, et al. (2006). "A mutation in RYK is a genetic factor for nonsyndromic cleft lip and palate.". Cleft Palate Craniofac. J. 43 (3): 310–6. doi:10.1597/04-145R1.1. PMID 16681403.
• Szafranski K, Schindler S, Taudien S, et al. (2007). "Violating the splicing rules: TG dinucleotides function as alternative 3' splice sites in U2-dependent introns.". Genome Biology 8 (8): R154. doi:10.1186/gb-2007-8-8-r154. PMC 2374985. PMID 17672918.