Receptor-type tyrosine-protein phosphatases (Homo sapiens)

From WikiPathways

Revision as of 16:05, 9 October 2020 by ReactomeTeam (Talk | contribs)
Jump to: navigation, search
119, 133, 6, 125, 101, 42, 87cytosolPresynapticPostsynapticcytosolSynaptic cleftPTPRS PTPRF LRRC4BSLITRK5 SLITRK2 Beta-liprins Alpha-liprins IL1RAPL2 Alpha-liprins SLITRK6 SLITRK4 SLITRK2 PTPRF NTRK3 Beta-liprins PTPRD PTPRF SLITRK1 IL1RAP-1 SLITRK4 PTPRD:IL1RAPL1,(IL1RAPL2)PTPRDSLITRK1-6:PTPRDPTPRS LAR,PTPRS,PTPRD:LiprinsLiprinsPTPRD IL1RAPL2 IL1RAPL1 SLITRK1 PTPRD PTPRD PTPRD IL1RAPL1 PTPRSPTPRS:NTRK3PTPRD:IL1RAP-1PTPRS PTPRD SLITRK3 SLITRK3 LRRC4B:PTPRF,PTPRS,PTPRDIL1RAPL1,(IL1RAPL2)PTPRS PTPRF, PTPRS, PTPRDSLITRK6 SLITRK1-6IL1RAP-1SLITRK5 NTRK3LRRC4B


Description

Like neurexins, Receptor-like protein tyrosine phosphatases (RPTPs) make trans-synaptic adhesion complexes with multiple postsynaptic binding partners to regulate synapse organization. The type IIa RPTPs include three members, Receptor-type tyrosine-protein phosphatase F (PTPRF) sometimes referred to as leukocyte common antigen-related (LAR), Receptor-type tyrosine-protein phosphatase sigma (PTPRS) and Receptor-type tyrosine-protein phosphatase delta (PTPRD). These proteins contain typical cell adhesion immunoglobulin-like (Ig) and fibronectin III (FNIII) domains, suggesting the involvement of RPTPs in cell-cell and cell-matrix interactions. To date, six different types of postsynaptic organizers for type-IIa RPTPs have been reported: interleukin-1 receptor accessory protein (IL1RAP, IL-1RAcP) (Yoshida et al. 2012), IL-1RAcP-like-1 (IL1RAPL1) (Yoshida et al. 2011), Neurotrophin receptor tyrosine kinase 3 (NTRK3, TrkC) (Takahashi et al. 2011), Leucine-rich repeat-containing protein 4B (LRRC4B, Netrin-G ligand-3, NGL-3) (Woo et al. 2009, Kwon et al. 2010), the Slit- and Trk-like (Slitrk) family proteins (Takahashi et al. 2012, Yim et al. 2013, Yamagata et al. 2015) and the liprins (Serra-Pagès et al. 1998, Dunah et al. 2005). View original pathway at:Reactome.

Comments

Reactome-Converter 
Pathway is converted from Reactome ID: 388844
Reactome-version 
Reactome version: 66
Reactome Author 
Reactome Author: Garapati, Phani Vijay

Try the New WikiPathways

View approved pathways at the new wikipathways.org.

Quality Tags

Ontology Terms

 

Bibliography

View all...
  1. Yoshida T, Shiroshima T, Lee SJ, Yasumura M, Uemura T, Chen X, Iwakura Y, Mishina M.; ''Interleukin-1 receptor accessory protein organizes neuronal synaptogenesis as a cell adhesion molecule.''; PubMed Europe PMC Scholia
  2. Takahashi H, Katayama K, Sohya K, Miyamoto H, Prasad T, Matsumoto Y, Ota M, Yasuda H, Tsumoto T, Aruga J, Craig AM.; ''Selective control of inhibitory synapse development by Slitrk3-PTPδ trans-synaptic interaction.''; PubMed Europe PMC Scholia
  3. Dunah AW, Hueske E, Wyszynski M, Hoogenraad CC, Jaworski J, Pak DT, Simonetta A, Liu G, Sheng M.; ''LAR receptor protein tyrosine phosphatases in the development and maintenance of excitatory synapses.''; PubMed Europe PMC Scholia
  4. Yoshida T, Yasumura M, Uemura T, Lee SJ, Ra M, Taguchi R, Iwakura Y, Mishina M.; ''IL-1 receptor accessory protein-like 1 associated with mental retardation and autism mediates synapse formation by trans-synaptic interaction with protein tyrosine phosphatase δ.''; PubMed Europe PMC Scholia
  5. Yamagata A, Yoshida T, Sato Y, Goto-Ito S, Uemura T, Maeda A, Shiroshima T, Iwasawa-Okamoto S, Mori H, Mishina M, Fukai S.; ''Mechanisms of splicing-dependent trans-synaptic adhesion by PTPδ-IL1RAPL1/IL-1RAcP for synaptic differentiation.''; PubMed Europe PMC Scholia
  6. Serra-Pagès C, Kedersha NL, Fazikas L, Medley Q, Debant A, Streuli M.; ''The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein co-localize at focal adhesions.''; PubMed Europe PMC Scholia
  7. Yim YS, Kwon Y, Nam J, Yoon HI, Lee K, Kim DG, Kim E, Kim CH, Ko J.; ''Slitrks control excitatory and inhibitory synapse formation with LAR receptor protein tyrosine phosphatases.''; PubMed Europe PMC Scholia
  8. Coles CH, Mitakidis N, Zhang P, Elegheert J, Lu W, Stoker AW, Nakagawa T, Craig AM, Jones EY, Aricescu AR.; ''Structural basis for extracellular cis and trans RPTPσ signal competition in synaptogenesis.''; PubMed Europe PMC Scholia
  9. Kwon SK, Woo J, Kim SY, Kim H, Kim E.; ''Trans-synaptic adhesions between netrin-G ligand-3 (NGL-3) and receptor tyrosine phosphatases LAR, protein-tyrosine phosphatase delta (PTPdelta), and PTPsigma via specific domains regulate excitatory synapse formation.''; PubMed Europe PMC Scholia
  10. Takahashi H, Arstikaitis P, Prasad T, Bartlett TE, Wang YT, Murphy TH, Craig AM.; ''Postsynaptic TrkC and presynaptic PTPσ function as a bidirectional excitatory synaptic organizing complex.''; PubMed Europe PMC Scholia
  11. Takahashi H, Craig AM.; ''Protein tyrosine phosphatases PTPδ, PTPσ, and LAR: presynaptic hubs for synapse organization.''; PubMed Europe PMC Scholia
  12. Woo J, Kwon SK, Choi S, Kim S, Lee JR, Dunah AW, Sheng M, Kim E.; ''Trans-synaptic adhesion between NGL-3 and LAR regulates the formation of excitatory synapses.''; PubMed Europe PMC Scholia
  13. Serra-Pagès C, Medley QG, Tang M, Hart A, Streuli M.; ''Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins.''; PubMed Europe PMC Scholia

History

View all...
CompareRevisionActionTimeUserComment
115024view16:56, 25 January 2021ReactomeTeamReactome version 75
113469view11:54, 2 November 2020ReactomeTeamReactome version 74
112667view16:05, 9 October 2020ReactomeTeamReactome version 73
101584view11:45, 1 November 2018ReactomeTeamreactome version 66
101120view21:29, 31 October 2018ReactomeTeamreactome version 65
100648view20:03, 31 October 2018ReactomeTeamreactome version 64
100198view16:47, 31 October 2018ReactomeTeamreactome version 63
99749view15:14, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99313view12:46, 31 October 2018ReactomeTeamreactome version 62
93303view11:19, 9 August 2017ReactomeTeamNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
Alpha-liprins R-HSA-383385 (Reactome)
Beta-liprins R-HSA-6799298 (Reactome)
IL1RAP-1 ProteinQ9NPH3-1 (Uniprot-TrEMBL)
IL1RAP-1ProteinQ9NPH3-1 (Uniprot-TrEMBL)
IL1RAPL1 ProteinQ9NZN1 (Uniprot-TrEMBL)
IL1RAPL1,(IL1RAPL2)ComplexR-HSA-6797845 (Reactome)
IL1RAPL2 ProteinQ9NP60 (Uniprot-TrEMBL)
LAR,PTPRS,PTPRD:LiprinsComplexR-HSA-383387 (Reactome)
LRRC4B ProteinQ9NT99 (Uniprot-TrEMBL)
LRRC4B:PTPRF,PTPRS,PTPRDComplexR-HSA-6798251 (Reactome)
LRRC4BProteinQ9NT99 (Uniprot-TrEMBL)
LiprinsComplexR-HSA-6799309 (Reactome)
NTRK3 ProteinQ16288 (Uniprot-TrEMBL)
NTRK3ProteinQ16288 (Uniprot-TrEMBL)
PTPRD ProteinP23468 (Uniprot-TrEMBL)
PTPRD:IL1RAP-1ComplexR-HSA-6800384 (Reactome)
PTPRD:IL1RAPL1,(IL1RAPL2)ComplexR-HSA-6797901 (Reactome)
PTPRDProteinP23468 (Uniprot-TrEMBL)
PTPRF ProteinP10586 (Uniprot-TrEMBL)
PTPRF, PTPRS, PTPRDComplexR-HSA-6798238 (Reactome)
PTPRS ProteinQ13332 (Uniprot-TrEMBL)
PTPRS:NTRK3ComplexR-HSA-6798231 (Reactome)
PTPRSProteinQ13332 (Uniprot-TrEMBL)
SLITRK1 ProteinQ96PX8 (Uniprot-TrEMBL)
SLITRK1-6:PTPRDComplexR-HSA-6797827 (Reactome)
SLITRK1-6ComplexR-HSA-6797785 (Reactome)
SLITRK2 ProteinQ9H156 (Uniprot-TrEMBL)
SLITRK3 ProteinO94933 (Uniprot-TrEMBL)
SLITRK4 ProteinQ8IW52 (Uniprot-TrEMBL)
SLITRK5 ProteinO94991 (Uniprot-TrEMBL)
SLITRK6 ProteinQ9H5Y7 (Uniprot-TrEMBL)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
IL1RAP-1R-HSA-6800380 (Reactome)
IL1RAPL1,(IL1RAPL2)R-HSA-6797810 (Reactome)
LAR,PTPRS,PTPRD:LiprinsArrowR-HSA-388824 (Reactome)
LRRC4B:PTPRF,PTPRS,PTPRDArrowR-HSA-6798258 (Reactome)
LRRC4BR-HSA-6798258 (Reactome)
LiprinsR-HSA-388824 (Reactome)
NTRK3R-HSA-6798257 (Reactome)
PTPRD:IL1RAP-1ArrowR-HSA-6800380 (Reactome)
PTPRD:IL1RAPL1,(IL1RAPL2)ArrowR-HSA-6797810 (Reactome)
PTPRDR-HSA-6797803 (Reactome)
PTPRDR-HSA-6797810 (Reactome)
PTPRDR-HSA-6800380 (Reactome)
PTPRF, PTPRS, PTPRDR-HSA-388824 (Reactome)
PTPRF, PTPRS, PTPRDR-HSA-6798258 (Reactome)
PTPRS:NTRK3ArrowR-HSA-6798257 (Reactome)
PTPRSR-HSA-6798257 (Reactome)
R-HSA-388824 (Reactome) All the three LAR-RPTP transmembrane tyrosine phosphatases associate with liprin proteins and colocalize with liprin-alpha1 at the proximal edges of focal adhesions. Based on sequence similarities and binding characteristics, liprins are subdivided into alpha-type and beta-type liprins. The C-terminal, non-coiled coil regions of alpha-liprins bind to the membrane-distal phosphatase domains of LAR family members, as well as to the C-terminal, non-coiled coil region of beta-liprins. Liprin is required for normal presynaptic differentiation in C. elegans and controls synapse morphogenesis in Drosophila. In mammalian synapses the functional significance of liprin and LAR-RPTP interaction is unknown (Pages et al. 1998, Dunah et al. 2005).
R-HSA-6797803 (Reactome) The SLIT and NTRK-like protein (SLITRK) family consists of six brain-specific transmembrane proteins (SLITRK1–6) that possess extracellular LRR domains homologous to the axon guidance molecule Slit and intracellular C-terminal tyrosine residues with surrounding sequences homologous to the Trk family (Aruga & Mikoshiba 2003). SLITRKs have been implicated in the modulation of neuronal process outgrowth promoting neuronal survival and in synapse formation (Linhoff et al. 2009). They exhibit synaptogenic activities through their interactions with specific LAR-RPTP members. All SLITRKs can interact with Receptor-type tyrosine-protein phosphatase delta (PTPRD), and SLIK1-3 at least can also interact with PTPRS (Meyer et al. 2004). SLITRK3 can induce inhibitory, but not excitatory, presynaptic differentiation whereas other family members induce both excitatory and inhibitory presynapses (Takahashi et al. 2012).
SLITRK1 variants are associated with Tourette’s syndrome (Abelson et al. 2005) and Trichotillomania (Zuchner et al. 2006) and obsessive compulsive disorders (OCDs). SLITRK2 is a candidate gene for schizophrenia (Piton et al. 2011) and bipolar disorder.
R-HSA-6797810 (Reactome) Interleukin-1 receptor accessory protein-like 1 (IL1RAPL1) belongs to the interleukin-1/Toll receptor family. It has extracellular Ig-like domains and an intracellular Toll/IL1R (TIR) domain. It regulates synapse formation of cortical neurons. Trans-synaptic interaction between postsynaptic IL1RAPL1 and presynaptic Receptor-type tyrosine-protein phosphatase delta (PTPRD) bidirectionally regulates excitatory synapse development. IL1RAPL2 is related to IL1RAPL1 and may also function in excitatory synapse organization although with less potency than IL1RAPL1 (Yoshida et al. 2011, Valnegri et al. 2011). IL1RAPL1 is associated with cognitive diseases ranging from nonsyndromic X-linked mental retardation to autism (Hayashi et al. 2013, Piton et al. 2008, Carrie et al. 1999).
R-HSA-6798257 (Reactome) Neurotrophin receptor 3 (NTRK3, TrkC) non-catalytic form acts as a synaptogenic adhesion molecule by binding to axonal Protein receptor-type tyrosine-protein phosphatase sigma (PTPRS). Transsynaptic interaction between dendritic NTRK3 and axonal PTPRS generates bidirectional non-catalytic signaling essential for excitatory pre- and postsynaptic differentiation in neural network development (Takahashi et al. 2011). The interaction between pre-synaptic PTPRS and post-synaptic NTRK3 involves extracellular domains of both proteins (Coles et al. 2014).
R-HSA-6798258 (Reactome) Leucine-rich repeat-containing protein 4B (LRRC4B, NGL-3) is a member of the netrin-G ligand (NGL, LRRC4) family that is widely expressed in the brain. LRRC4B binds with high affinity to Protein tyrosine Receptor-type tyrosine-protein phosphatase F (PTPRF, LAR), Protein tyrosine Receptor-type tyrosine-protein phosphatase sigma (PTPRS) and Protein tyrosine Receptor-type tyrosine-protein phosphatase delta (PTPRD). It binds to the first two fibronectin III (FnIII) domains of the PTPRs, thus it is likely to interact with all PTPRs splice variants. LRRC4B may induce both excitatory and inhibitory presynaptic differentiation in contacting axons (Woo et al. 2009, 2010).
R-HSA-6800380 (Reactome) Receptor protein tyrosine phosphatase delta (PTPRD) can bidirectionally induce pre- and postsynaptic differentiation of neurons by trans-synaptically binding to interleukin-1 receptor accessory protein (IL1RAP) (Yoshida et al. 2012, Yamagata et al. 2015). IL1RAP has two distinct functions, one in immune regulation and inflammation by associating with IL1 and IL1R1 and another with PTPRD in synaptic adhesion and synapse organization (Dunne & O'Neill 2003).
SLITRK1-6:PTPRDArrowR-HSA-6797803 (Reactome)
SLITRK1-6R-HSA-6797803 (Reactome)
Retrieved from "https://classic.wikipathways.org/index.php/Pathway:WP4046"
Personal tools