Signaling by ROBO receptors (Homo sapiens)
From WikiPathways
Description
The Roundabout (Robo) family encodes transmembrane receptors that regulate axonal guidance and cell migration. The major function of the Robo receptors is to mediate repulsion of the navigating growth cones. There are four human Robo homologues, Robo1, Robo2, Robo3 and Robo4. Most of the Robos have the similar ectodomain architecture as the cell adhesion molecules, five Ig domains followed by three FN3 repeats except for Robo4, it has 2Ig and 2FN3 repeats. The cytoplasmic domains of Robo receptors are in general poorly conserved. However, there are four short conserved cytoplasmic sequence motifs, named CC0-3, that serve as binding sites for adaptor proteins. The ligands for the human Robo receptors are the three Slit proteins Slit1, Slit2, and Slit3; all of the Slit proteins contain a tandem of four LRR (leucine rich repeat) domains at N terminus, termed D1 D4 followed by six EGF (epidermal growth factor)-like domains, a laminin G like domain (ALPS), three EGF-like domains, and a C-terminal cysteine knot domain. Most Slit proteins are cleaved within the EGF-like region by unknown proteases.
Slit protein binding modulates Robo interactions with the cytosolic adaptors. The cytoplasmic domain of Robo1 and Robo2 determines the repulsive responses of these receptors. Based on the studies from both invertebrate and vertebrate organisms its been inferred that Robo induces growth cone repulsion by controlling cytoskeletal dynamics via either Abelson kinase (Abl) and Enabled (Ena), or Rac activity.
Original Pathway at Reactome: http://www.reactome.org/PathwayBrowser/#DB=gk_current&FOCUS_SPECIES_ID=48887&FOCUS_PATHWAY_ID=376176
Slit protein binding modulates Robo interactions with the cytosolic adaptors. The cytoplasmic domain of Robo1 and Robo2 determines the repulsive responses of these receptors. Based on the studies from both invertebrate and vertebrate organisms its been inferred that Robo induces growth cone repulsion by controlling cytoskeletal dynamics via either Abelson kinase (Abl) and Enabled (Ena), or Rac activity.
Original Pathway at Reactome: http://www.reactome.org/PathwayBrowser/#DB=gk_current&FOCUS_SPECIES_ID=48887&FOCUS_PATHWAY_ID=376176
Quality Tags
Ontology Terms
Saving...Bibliography
View all... |
- Mire E, Mezzera C, Leyva-Díaz E, Paternain AV, Squarzoni P, Bluy L, Castillo-Paterna M, López MJ, Peregrín S, Tessier-Lavigne M, Garel S, Galcerán J, Lerma J, López-Bendito G.; ''Spontaneous activity regulates Robo1 transcription to mediate a switch in thalamocortical axon growth.''; PubMed Europe PMC Scholia
- Chan PM, Manser E.; ''PAKs in human disease.''; PubMed Europe PMC Scholia
- Leung T, Chen XQ, Manser E, Lim L.; ''The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton.''; PubMed Europe PMC Scholia
- Nicholson P, Yepiskoposyan H, Metze S, Zamudio Orozco R, Kleinschmidt N, Mühlemann O.; ''Nonsense-mediated mRNA decay in human cells: mechanistic insights, functions beyond quality control and the double-life of NMD factors.''; PubMed Europe PMC Scholia
- Bhuvanagiri M, Schlitter AM, Hentze MW, Kulozik AE.; ''NMD: RNA biology meets human genetic medicine.''; PubMed Europe PMC Scholia
- Dutil EM, Toker A, Newton AC.; ''Regulation of conventional protein kinase C isozymes by phosphoinositide-dependent kinase 1 (PDK-1).''; PubMed Europe PMC Scholia
- Round JE, Sun H.; ''The adaptor protein Nck2 mediates Slit1-induced changes in cortical neuron morphology.''; PubMed Europe PMC Scholia
- Conrad AH, Zhang Y, Tasheva ES, Conrad GW.; ''Proteomic analysis of potential keratan sulfate, chondroitin sulfate A, and hyaluronic acid molecular interactions.''; PubMed Europe PMC Scholia
- Szczepanowska J.; ''Involvement of Rac/Cdc42/PAK pathway in cytoskeletal rearrangements.''; PubMed Europe PMC Scholia
- Chang YF, Imam JS, Wilkinson MF.; ''The nonsense-mediated decay RNA surveillance pathway.''; PubMed Europe PMC Scholia
- Li L, Liu S, Lei Y, Cheng Y, Yao C, Zhen X.; ''Robo3.1A suppresses slit-mediated repulsion by triggering degradation of Robo2.''; PubMed Europe PMC Scholia
- Prasad A, Qamri Z, Wu J, Ganju RK.; ''Slit-2/Robo-1 modulates the CXCL12/CXCR4-induced chemotaxis of T cells.''; PubMed Europe PMC Scholia
- Durand S, Lykke-Andersen J.; ''SnapShot: Nonsense-mediated mRNA decay.''; PubMed Europe PMC Scholia
- Blockus H, Chédotal A.; ''Slit-Robo signaling.''; PubMed Europe PMC Scholia
- Sumi T, Matsumoto K, Nakamura T.; ''Specific activation of LIM kinase 2 via phosphorylation of threonine 505 by ROCK, a Rho-dependent protein kinase.''; PubMed Europe PMC Scholia
- Jaworski A, Tom I, Tong RK, Gildea HK, Koch AW, Gonzalez LC, Tessier-Lavigne M.; ''Operational redundancy in axon guidance through the multifunctional receptor Robo3 and its ligand NELL2.''; PubMed Europe PMC Scholia
- Wang KH, Brose K, Arnott D, Kidd T, Goodman CS, Henzel W, Tessier-Lavigne M.; ''Biochemical purification of a mammalian slit protein as a positive regulator of sensory axon elongation and branching.''; PubMed Europe PMC Scholia
- Stalder L, Mühlemann O.; ''The meaning of nonsense.''; PubMed Europe PMC Scholia
- Wang J, Wu JW, Wang ZX.; ''Mechanistic studies of the autoactivation of PAK2: a two-step model of cis initiation followed by trans amplification.''; PubMed Europe PMC Scholia
- Samelson BK, Gore BB, Whiting JL, Nygren PJ, Purkey AM, Colledge M, Langeberg LK, Dell'Acqua ML, Zweifel LS, Scott JD.; ''A-kinase Anchoring Protein 79/150 Recruits Protein Kinase C to Phosphorylate Roundabout Receptors.''; PubMed Europe PMC Scholia
- Brose K, Bland KS, Wang KH, Arnott D, Henzel W, Goodman CS, Tessier-Lavigne M, Kidd T.; ''Slit proteins bind Robo receptors and have an evolutionarily conserved role in repulsive axon guidance.''; PubMed Europe PMC Scholia
- Jung JH, Traugh JA.; ''Regulation of the interaction of Pak2 with Cdc42 via autophosphorylation of serine 141.''; PubMed Europe PMC Scholia
- Amano M, Nakayama M, Kaibuchi K.; ''Rho-kinase/ROCK: A key regulator of the cytoskeleton and cell polarity.''; PubMed Europe PMC Scholia
- Neu-Yilik G, Kulozik AE.; ''NMD: multitasking between mRNA surveillance and modulation of gene expression.''; PubMed Europe PMC Scholia
- Manser E, Leung T, Salihuddin H, Zhao ZS, Lim L.; ''A brain serine/threonine protein kinase activated by Cdc42 and Rac1.''; PubMed Europe PMC Scholia
- Zhang B, Dietrich UM, Geng JG, Bicknell R, Esko JD, Wang L.; ''Repulsive axon guidance molecule Slit3 is a novel angiogenic factor.''; PubMed Europe PMC Scholia
- Ypsilanti AR, Chedotal A.; ''Roundabout receptors.''; PubMed Europe PMC Scholia
- Amano M, Ito M, Kimura K, Fukata Y, Chihara K, Nakano T, Matsuura Y, Kaibuchi K.; ''Phosphorylation and activation of myosin by Rho-associated kinase (Rho-kinase).''; PubMed Europe PMC Scholia
- Zhang F, Ronca F, Linhardt RJ, Margolis RU.; ''Structural determinants of heparan sulfate interactions with Slit proteins.''; PubMed Europe PMC Scholia
- Hohenester E.; ''Structural insight into Slit-Robo signalling.''; PubMed Europe PMC Scholia
- Daniels RH, Bokoch GM.; ''p21-activated protein kinase: a crucial component of morphological signaling?''; PubMed Europe PMC Scholia
- Isken O, Maquat LE.; ''Quality control of eukaryotic mRNA: safeguarding cells from abnormal mRNA function.''; PubMed Europe PMC Scholia
- Bashaw GJ, Kidd T, Murray D, Pawson T, Goodman CS.; ''Repulsive axon guidance: Abelson and Enabled play opposing roles downstream of the roundabout receptor.''; PubMed Europe PMC Scholia
- Piper M, Little M.; ''Movement through Slits: cellular migration via the Slit family.''; PubMed Europe PMC Scholia
- Graf B, Bähler M, Hilpelä P, Böwe C, Adam T.; ''Functional role for the class IX myosin myr5 in epithelial cell infection by Shigella flexneri.''; PubMed Europe PMC Scholia
- Kong R, Yi F, Wen P, Liu J, Chen X, Ren J, Li X, Shang Y, Nie Y, Wu K, Fan D, Zhu L, Feng W, Wu JY.; ''Myo9b is a key player in SLIT/ROBO-mediated lung tumor suppression.''; PubMed Europe PMC Scholia
- Voges D, Zwickl P, Baumeister W.; ''The 26S proteasome: a molecular machine designed for controlled proteolysis.''; PubMed Europe PMC Scholia
- Post PL, Bokoch GM, Mooseker MS.; ''Human myosin-IXb is a mechanochemically active motor and a GAP for rho.''; PubMed Europe PMC Scholia
- Rebbapragada I, Lykke-Andersen J.; ''Execution of nonsense-mediated mRNA decay: what defines a substrate?''; PubMed Europe PMC Scholia
- Zhang B, Chernoff J, Zheng Y.; ''Interaction of Rac1 with GTPase-activating proteins and putative effectors. A comparison with Cdc42 and RhoA.''; PubMed Europe PMC Scholia
- Borrell V, Cárdenas A, Ciceri G, Galcerán J, Flames N, Pla R, Nóbrega-Pereira S, García-Frigola C, Peregrín S, Zhao Z, Ma L, Tessier-Lavigne M, Marín O.; ''Slit/Robo signaling modulates the proliferation of central nervous system progenitors.''; PubMed Europe PMC Scholia
- Ronca F, Andersen JS, Paech V, Margolis RU.; ''Characterization of Slit protein interactions with glypican-1.''; PubMed Europe PMC Scholia
- Bravo-Ambrosio A, Mastick G, Kaprielian Z.; ''Motor axon exit from the mammalian spinal cord is controlled by the homeodomain protein Nkx2.9 via Robo-Slit signaling.''; PubMed Europe PMC Scholia
- Wei SJ, Williams JG, Dang H, Darden TA, Betz BL, Humble MM, Chang FM, Trempus CS, Johnson K, Cannon RE, Tennant RW.; ''Identification of a specific motif of the DSS1 protein required for proteasome interaction and p53 protein degradation.''; PubMed Europe PMC Scholia
- Parrini MC, Lei M, Harrison SC, Mayer BJ.; ''Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.''; PubMed Europe PMC Scholia
- Zhao ZS, Manser E, Lim L.; ''Interaction between PAK and nck: a template for Nck targets and role of PAK autophosphorylation.''; PubMed Europe PMC Scholia
- Manser E, Chong C, Zhao ZS, Leung T, Michael G, Hall C, Lim L.; ''Molecular cloning of a new member of the p21-Cdc42/Rac-activated kinase (PAK) family.''; PubMed Europe PMC Scholia
- Ishizaki T, Maekawa M, Fujisawa K, Okawa K, Iwamatsu A, Fujita A, Watanabe N, Saito Y, Kakizuka A, Morii N, Narumiya S.; ''The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase.''; PubMed Europe PMC Scholia
- Huang Z, Wen P, Kong R, Cheng H, Zhang B, Quan C, Bian Z, Chen M, Zhang Z, Chen X, Du X, Liu J, Zhu L, Fushimi K, Hua D, Wu JY.; ''USP33 mediates Slit-Robo signaling in inhibiting colorectal cancer cell migration.''; PubMed Europe PMC Scholia
- Keranen LM, Dutil EM, Newton AC.; ''Protein kinase C is regulated in vivo by three functionally distinct phosphorylations.''; PubMed Europe PMC Scholia
- Behm-Ansmant I, Kashima I, Rehwinkel J, Saulière J, Wittkopp N, Izaurralde E.; ''mRNA quality control: an ancient machinery recognizes and degrades mRNAs with nonsense codons.''; PubMed Europe PMC Scholia
- Yuasa-Kawada J, Kinoshita-Kawada M, Rao Y, Wu JY.; ''Deubiquitinating enzyme USP33/VDU1 is required for Slit signaling in inhibiting breast cancer cell migration.''; PubMed Europe PMC Scholia
- Chong C, Tan L, Lim L, Manser E.; ''The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity.''; PubMed Europe PMC Scholia
- Ohashi K, Nagata K, Maekawa M, Ishizaki T, Narumiya S, Mizuno K.; ''Rho-associated kinase ROCK activates LIM-kinase 1 by phosphorylation at threonine 508 within the activation loop.''; PubMed Europe PMC Scholia
- Kadlec J, Izaurralde E, Cusack S.; ''The structural basis for the interaction between nonsense-mediated mRNA decay factors UPF2 and UPF3.''; PubMed Europe PMC Scholia
- Kimura K, Ito M, Amano M, Chihara K, Fukata Y, Nakafuku M, Yamamori B, Feng J, Nakano T, Okawa K, Iwamatsu A, Kaibuchi K.; ''Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase)''; PubMed Europe PMC Scholia
- Lei M, Lu W, Meng W, Parrini MC, Eck MJ, Mayer BJ, Harrison SC.; ''Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch.''; PubMed Europe PMC Scholia
- Watanabe T, Hosoya H, Yonemura S.; ''Regulation of myosin II dynamics by phosphorylation and dephosphorylation of its light chain in epithelial cells.''; PubMed Europe PMC Scholia
History
View all... |
External references
DataNodes
| View all... |
Annotated Interactions
| View all... |
| Source | Target | Type | Database reference | Comment |
|---|---|---|---|---|
| ADP | Arrow | REACT_19227 (Reactome)  | ||
| ARHGAP39 | REACT_19229 (Reactome) | |||
| ATP | REACT_19227 (Reactome) | |||
| Abl
Robo1 Slit2 Glypican-1 | REACT_19182 (Reactome) | |||
| Abl
Robo1 Slit2 Glypican-1 | REACT_19227 (Reactome) | |||
| Abl
Robo1 Slit2 Glypican-1 | REACT_19260 (Reactome) | |||
| Abl
Robo1 Slit2 Glypican-1 | mim-catalysis | REACT_19227 (Reactome) | ||
| Abl
pRobo1 slit2 Glypican-1 | Arrow | REACT_19227 (Reactome) | ||
| Abl tyrosine kinases | REACT_19396 (Reactome) | |||
| CAP | REACT_19260 (Reactome) | |||
| CDC42-GDP | Arrow | REACT_19125 (Reactome) | ||
| CLASP | REACT_19182 (Reactome) | |||
| Ena/Vasp proteins | REACT_19132 (Reactome) | |||
| GDP | Arrow | REACT_19252 (Reactome) | ||
| GTP | REACT_19252 (Reactome) | |||
| Glypican-1 HSPG | REACT_19262 (Reactome) | |||
| Glypican-1
Slit2 Robo1 Ena/Vasp proteins | REACT_19293 (Reactome) | |||
| NCK | REACT_19119 (Reactome) | |||
| Nck
Robo1 Slit2 Glypican | REACT_19217 (Reactome) | |||
| PAK | REACT_19217 (Reactome) | |||
| Pak
Nck Robo1 Slit2 Glypican | REACT_19355 (Reactome) | |||
| Pi | Arrow | REACT_19125 (Reactome) | ||
| Pi | Arrow | REACT_19359 (Reactome) | ||
| Profilin | REACT_19293 (Reactome) | |||
| RAC1-GDP | Arrow | REACT_19359 (Reactome) | ||
| RAC1-GDP | REACT_19252 (Reactome) | |||
| RAC1-GTP | Arrow | REACT_19252 (Reactome) | ||
| REACT_19119 (Reactome) | Slit stimulation recruits SH3 SH2 adaptor protein Dreadlocks (Dock) (Nck in vertebrates) to the Robo receptor. | |||
| REACT_19125 (Reactome) | srGAP bound to Robo's cytoplasmic tail increase the intrinsic GTPase activity of Cdc42, which converts the GTP-bound form of Cdc42 into its GDP-bound form, therefore inactivating Cdc42. Inactivation of Cdc42 leads to a reduction in the activation of the Neuronal WiskottAldrich Syndrome protein (NWASP), thus decreasing the level of active Arp2/3 complex. Because active Arp2/3 promotes actin polymerization, the reduction of active Cdc42 eventually decreases actin polymerization. Slit regulates SrGAP interaction with Robo1 and Cdc42, it increases SrGAP interaction with Cdc42. | |||
| REACT_19132 (Reactome) | Ena is required in part for Robo's repulsive output. Ena is drawn as an effector downstream of Robo signaling via a direct interaction with Robo. Robo's CC2 (LPPPP) motif is the consensus binding site for the EVH1 domain of Ena. The Ena/VASP family of proteins has a universal role in control of cell motility and actin dynamics. These proteins consist of an N terminal EVH1 domain, a central proline rich region, which acts as a ligand for the actin monomer binding protein Profilin as well as several SH3 domain containing proteins including Abl and a C terminal EVH2 domain involved in oligomerization and F actin binding. | |||
| REACT_19182 (Reactome) | CLASP acts positively downstream of Abl as part of the repellent response initiated by activation of Robo1. CLASP is spatially positioned to interact with Robo receptors. Slit mediated repulsion results in activation of CLASP, presumably through its phosphorylation by the Abl kinase. Activation of CLASP in turn results in inhibition of microtubule polymerization on the side of the growth cone receiving the repulsive signal and consequently the growth cone turns to the opposite side. A direct link between Abl and CLASP, notably the mechanism of CLASP activation, has not been demonstrated, however. | |||
| REACT_19205 (Reactome) | Robo3 antagonizes Robo1/Robo2 function to prevent their response to slit, thus allowing cells that are expressing Robo1/Robo2 to progress towards and across the floor plate. Exactly how Robo3 interferes with Robo1/Robo2 function is not yet clear. One possibility is that one of the Robo3 isoform Robo3A.1 may sequester Robo1 into inactive receptor complexes. Robo3 in mouse and human have two isoforms, Robo3A.1 and Robo3A.2 with different Slit-binding activities. Both isoforms can form heterodimers with Robo1 and Robo2, but Robo3A.1 heterodimers cannot bind Slit, so this isoform may serve to sequester and inactivate Robo1. | |||
| REACT_19217 (Reactome) | Dock/Nck bound to Robo recruits Pak to specific sites at the growth cone membrane, where Pak, activated by Rac, regulates the recycling and retrograde flow of actin filaments. [In mammals there are six PAK isoforms and PAK binds to the 2nd SH3 domain of Nck with its proline rich PxxP motif.] | |||
| REACT_19227 (Reactome) | Abl kinase phosphorylates the tyrosine residue (1073) of the conserved CC1 motif (PTPYATT) in human Robo1. | |||
| REACT_19229 (Reactome) | Vilse/CrossGAP (CrGAP) a conserved Rac-Specific GAP in Drosophila is involved in Robo mediated repulsion. CrGAP directly binds to Robo both biochemically and genetically. This interaction is mediated by the WW domains in CrGAP and the CC2 motif of Robo. The human homologue of Vilse/CrGAP, KIAA1688, was identified which shares 54.4% sequence similarity with Drosophila CrGAP and is referred as human Vilse/CrGAP protein. | |||
| REACT_19252 (Reactome) | Sos bound to Dock/Nck, with its Rac GEF activity activates Rac. Son of sevenless (Sos) is a dual specificity guanine nucleotide exchange factor (GEF) that regulates both Ras and Rho family GTPases. The Ras and Rac-GEF activities of Sos can be uncoupled during Robo-mediated axon repulsion; Sos axon guidance function depends on its Rac-GEF activity, but not its Ras-GEF activity. | |||
| REACT_19260 (Reactome) | Abl associated with Robo1, Slit2, and glypican at the plasma membrane binds CAP and regulate its activity to inhibit net actin assembly. Studies of CAP homologs from yeast, Dictyostelium, mouse, pig, and human suggest that the C terminal actin binding domain acts to sequester monomers to prevent actin polymerization. | |||
| REACT_19262 (Reactome) | Slit 2 and both its natural cleavage products bind glypican 1, a glycosyl phosphatidyl inositol (GPI) anchored heparan sulfate proteoglycan (HSPG) through its C terminus. Glypican 1 HSPG is important for high affinity binding of Slit to its receptor and for the repulsive activity of Slit. Slit-Robo signaling strictly requires binding to heparan sulfate. HSPGs may also modulate the extracellular distribution or stability of Slit proteins. | |||
| REACT_19272 (Reactome) | The Slit family consists of three members that are all expressed in the ventral midline (floor plate) of the neural tube. Slit 1 is predominantly expressed in the nervous system whereas Slit 2 and 3 are also expressed outside the nervous system. Slit proteins are the ligands for the Robo receptors. In humans there are four robo genes: Robo1, 2, 3 and 4. The extracellular domain of Robo comprises five Ig domains and three Fn domains except for Robo4 (2Ig+2Fn). Ig1 and Ig2 domains of Robo are highly conserved and are important for Slit binding. The concave face of slit's second LRR domain accommodates the Robo's Ig1 and 2 domains. Slit binding with Robo4 is controversial as the interaction is weak and its been observed using the in-vitro methods. | |||
| REACT_19280 (Reactome) | The Robo1 receptor regulates Rho GTPase activity through a ligand-dependent association with members of a novel family of GAPs called srGAPs (slit-robo GAPs). Extracellular interaction between Slit and Robo increases the intracellular interaction between the CC3 motif of Robo1 and the SH3 motif of the SrGAPs. | |||
| REACT_19284 (Reactome) | The full length Slit proteins are membrane bound via the extracellular matrix proteins when not bound to Robo receptors. These full length Slits undergo post translational modification and proteolytic processing to generate an N terminal fragment (Slit2 N) and a corresponding C terminal fragment (Slit2 C). Slit 2 is cleaved within the EGF repeats, between EGF5 and EGF6, by unknown proteases. Cleavage of Slit proteins is evolutionarily conserved, although the molecular biological significance is unknown. The N-terminal fragment of Slit2 stimulates growth and branching of dorsal root ganglia (DRG) axons, and this activity is opposed by un-cleaved Slit. The stimulation of axon branching is mediated by Robo receptors. Additional functional differences between the full-length and N-terminal forms have been discovered in their abilities to repel different populations of axons and dendrites. Finally, Slit can attract migrating muscles in the fly, and also human endothelial cells, both via Robo receptors. | |||
| REACT_19293 (Reactome) | Ena/VASP proteins enhance actin filament elongation via the recruitment of profilin:actin complexes to the tips of spreading lamellipodia. Profilin binds to the central proline rich domain of Ena/VASP protein. | |||
| REACT_19355 (Reactome) | Upon Slit stimulation Sos is recruited into the multiprotein complex consisting of Robo, the SH3-SH2 protein Dock/Nck, and Sos, in which Dock/Nck bridges the physical association between Robo and Sos. | |||
| REACT_19359 (Reactome) | Vilse and its human homolog bind directly to the intracellular domains of the corresponding Robo receptors and promote the hydrolysis of RacGTP. | |||
| REACT_19396 (Reactome) | Abl binds directly, via its SH3 domain, to the CC3 motif in the cytoplasmic domain of human Robo1. | |||
| ROBO1 | REACT_19272 (Reactome) | |||
| ROBO3-1 | REACT_19205 (Reactome) | |||
| Robo1
Slit2 Glypican-1 | REACT_19119 (Reactome) | |||
| Robo1
Slit2 Glypican-1 | REACT_19132 (Reactome) | |||
| Robo1
Slit2 Glypican-1 | REACT_19229 (Reactome) | |||
| Robo1
Slit2 Glypican-1 | REACT_19280 (Reactome) | |||
| Robo1
Slit2 Glypican-1 | REACT_19396 (Reactome) | |||
| Robo1
Slit2 KIAA1688 | mim-catalysis | REACT_19359 (Reactome) | ||
| Robo1
Slit2 SrGAP | mim-catalysis | REACT_19125 (Reactome) | ||
| Robo1/ Robo2 | REACT_19205 (Reactome) | |||
| SLIT2 | Arrow | REACT_19284 (Reactome) | ||
| SLIT2 | REACT_19262 (Reactome) | |||
| SOS
PAK Nck Robo1 Slit2 Glypican | mim-catalysis | REACT_19252 (Reactome) | ||
| SOS | REACT_19355 (Reactome) | |||
| Slit2 Glypican-1 | REACT_19272 (Reactome) | |||
| SrGAP | REACT_19280 (Reactome) | |||
| Unidentified protease | mim-catalysis | REACT_19284 (Reactome) |
