Related to receptor tyrosine kinase

RYK
Identifiers
Aliases	RYK , D3S3195, JTK5, JTK5A, RYK1, receptor-like tyrosine kinase, receptor like tyrosine kinase
External IDs	OMIM: 600524 MGI: 101766 HomoloGene: 68287 GeneCards: RYK
Gene location (Human) Chr. Chromosome 3 (human) [1] Band 3q22.2 Start 134,065,303 bp [1] End 134,250,859 bp [1]
Gene location (Mouse) Chr. Chromosome 9 (mouse) [2] Band 9 F1|9 54.72 cM Start 102,712,116 bp [2] End 102,785,504 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Achilles tendon saphenous vein gastric mucosa urethra germinal epithelium stromal cell of endometrium synovial joint pericardium tibia vena cava Top expressed in secondary oocyte lip calvaria molar renal corpuscle saccule esophagus belly cord epidermis hair follicle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function nucleotide binding protein tyrosine kinase activity transferase activity transmembrane signaling receptor activity kinase activity Wnt-activated receptor activity ATP binding protein binding frizzled binding Wnt-protein binding coreceptor activity involved in Wnt signaling pathway, planar cell polarity pathway receptor tyrosine kinase transmembrane receptor protein tyrosine kinase activity protein kinase activity Cellular component cytoplasm integral component of membrane integral component of plasma membrane membrane plasma membrane nucleus receptor complex Biological process positive regulation of MAPK cascade corpus callosum development signal transduction canonical Wnt signaling pathway non-canonical Wnt signaling pathway neurogenesis commissural neuron axon guidance neuron projection development protein phosphorylation synapse assembly chemorepulsion of dopaminergic neuron axon neuron differentiation cell proliferation in midbrain phosphorylation axonogenesis axon guidance Wnt signaling pathway involved in midbrain dopaminergic neuron differentiation midbrain dopaminergic neuron differentiation planar cell polarity pathway involved in axon guidance Wnt signaling pathway peptidyl-tyrosine phosphorylation skeletal system morphogenesis negative regulation of axon extension involved in axon guidance negative chemotaxis negative regulation of signal transduction cell differentiation negative regulation of apoptotic process positive regulation of ERK1 and ERK2 cascade transmembrane receptor protein tyrosine kinase signaling pathway nervous system development Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6259 20187 Ensembl ENSG00000163785 ENSMUSG00000032547 UniProt P34925 Q01887 RefSeq (mRNA) NM_001005861 NM_002958 NM_001042607 NM_013649 NM_001284258 RefSeq (protein) NP_001005861 NP_002949 NP_001036072 NP_001271187 NP_038677 Location (UCSC) Chr 3: 134.07 – 134.25 Mb Chr 9: 102.71 – 102.79 Mb PubMed search [3] [4]
Wikidata
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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. ^[5]

History

The gene encoding mouse RYK was first identified in 1992. ^[6] Subsequently, cDNA encoding the RYK protein have been isolated from the following species. ^[7]

• rat
• chicken
• Human
• Zebrafish
• Caenorhabditis elegans
• Drosophila

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. ^[7]

Function

RYK is involved in regulation of axon growth during development of the nervous system. ^[8]

References

1. GRCh38: Ensembl release 89: ENSG00000163785 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000032547 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "RYK receptor like tyrosine kinase [Homo sapiens (human) ]". National Center for Biotechnology Information, U.S. National Library of Medicine. 13 March 2020. Retrieved 2 April 2020.
6. 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. Bibcode:1992PNAS...8911818H. doi: 10.1073/pnas.89.24.11818 . PMC   50648 . PMID   1334548.
7. Halford MM, Stacker SA (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. S2CID   18535933.
8. 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 (2016). "Ryk controls remapping of motor cortex during functional recovery after spinal cord injury". Nature Neuroscience. 19 (5): 697–705. doi:10.1038/nn.4282. PMC   4847956 . PMID   27065364.

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. S2CID   2577241.
• 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. doi:10.1007/BF03401616. 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. doi:10.1128/mcb.19.9.6427. 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. Bibcode:2002PNAS...9916899M. 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. S2CID   27764390.
• 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. S2CID   18567677.
• 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:10.1597/04-145.1. PMID   16681403. S2CID   23152169.
• 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.