The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
Identity is verified. The requested target is human GRB2, approved name growth factor receptor-bound protein 2 (UniProt P62993; Ensembl ENSG00000177885), not the related proteins GAB1, GAB2, GRAP2, or SH3GL family members. The literature describes the same 217-amino-acid, approximately 25-kDa protein and explicitly uses P62993 in recent experimental work. Its architecture—an N-terminal SH3 domain, central SH2 domain, and C-terminal SH3 domain—matches the supplied InterPro annotation and the GRB2/sem-5/DRK family. No organism or symbol conflict was found. (OpenTargets Search: -GRB2, wang2024theconfigurationof pages 1-2, nocka2023stimulationofthe pages 11-13)
GRB2 is not an enzyme or transporter. It is a compact, non-catalytic signaling adaptor that converts phosphorylation patterns into spatially organized protein complexes. Its SH2 domain docks on phosphotyrosine-containing receptor or scaffold motifs, whereas its two SH3 domains recruit proline-rich effectors. The best-established output is placement of the RAS guanine-nucleotide-exchange factor SOS next to membrane-bound RAS, thereby activating the RAS–RAF–MEK–ERK pathway. GRB2 also couples receptors to Gab scaffolds, PI3K–AKT signaling, immune-receptor complexes, cytoskeletal machinery, and receptor endocytosis. Recent work extends this classical “molecular bridge” model: GRB2 can relieve BTK autoinhibition at PIP3-containing membranes and can partition into oncogenic CCDC6–RET/SHC1 condensate-like signaling niches. (wang2024theconfigurationof pages 2-4, wang2024theconfigurationof pages 1-2, nocka2023stimulationofthe pages 11-13, qiu2024ccdc6retfusionprotein pages 8-9)
Human GRB2 comprises 217 residues and is approximately 25 kDa. A 2024 annotation places the N-terminal SH3 domain at residues 1–58, the central SH2 domain at 60–152, and the C-terminal SH3 domain at 156–215. This is the expected SH3–SH2–SH3 organization; some sources reverse “N-SH3” and “C-SH3” labels when describing residue order, but the physical architecture is unambiguous. A full-length crystal structure has been reported at 3.1-Å resolution (PDB 1GR1). (wang2024theconfigurationof pages 1-2, malagrino2024grb2adynamic pages 2-3)
The primary function of GRB2 is to assemble and spatially position signaling complexes. In the canonical pathway:
Accordingly, GRB2 has no catalytic reaction or substrate specificity in the enzymatic sense. Its functional specificity is interaction specificity: phosphotyrosine-sequence recognition by SH2 and proline-rich-sequence recognition by SH3. Its broader structural role is to bridge activated receptors or scaffolds to cytoplasmic effectors and to increase their local concentration at the correct membrane or signaling assembly.
The RTK–GRB2–SOS–RAS axis is the most firmly established GRB2 pathway. It operates downstream of EGFR and many other RTKs, either by direct receptor binding or through SHC. The mechanism explains how extracellular growth factors are translated into ERK-dependent transcriptional and cellular responses. It also explains why GRB2 is repeatedly implicated in cancers driven by receptor activation, RAS-pathway amplification, or constitutively active tyrosine-kinase fusions. (wang2024theconfigurationof pages 1-2, wang2024theconfigurationof pages 9-11, malagrino2024grb2adynamic pages 3-3)
GRB2 can also restrain signaling in a receptor-specific state. Structural and biochemical studies summarized in 2024 indicate that unstimulated FGFR2 can form a heterotetramer with GRB2, stabilizing a predimerized receptor while suppressing receptor phosphorylation and MAPK output. FGF stimulation promotes kinase activity and GRB2 Tyr209 phosphorylation, followed by complex dissociation. This illustrates that GRB2 is not invariably an “on switch”; its effect depends on partner, phosphorylation state, and complex configuration. (wang2024theconfigurationof pages 11-12)
GRB2’s C-terminal SH3 domain binds Gab-family docking proteins. Recruitment of Gab1 downstream of activated RTKs creates additional phosphotyrosine docking sites and connects receptor signaling to PI3K–AKT survival pathways. This branch is mechanistically parallel to, rather than synonymous with, GRB2–SOS–RAS signaling. (wang2024theconfigurationof pages 2-4, malagrino2024grb2adynamic pages 3-3)
A major recent mechanistic advance came from a 2023 eLife study using supported lipid bilayers. PIP3 recruited full-length BTK to membranes; membrane-bound BTK then recruited GRB2 through BTK’s 44-residue proline-rich linker, which contains ten prolines and two PxxP motifs. Recruitment required intact GRB2 containing both SH3 domains and the intervening SH2 domain, although the SH2 domain did not need phosphotyrosine-binding activity. GRB2 relieved BTK autoinhibition, recruited BTK to LAT signaling clusters, and accelerated phosphorylation of a PLCγ2 segment. GRB2 did not measurably increase the BTK dimer population, arguing that conformational release—not additional dimerization—was the main activating mechanism. (nocka2023stimulationofthe pages 11-13, nocka2023stimulationofthe pages 1-2)
Quantitatively, these assays used bilayers containing 4% PIP3; complementary His-tag tethering assays used 4% DGS-NTA(Ni). Tested BTK constructs included full length, residues 212–659, 281–659, 402–659, and the isolated proline-rich linker at residues 171–214. The fluorescence-labeling fraction for GRB2 was approximately 17%. These are direct reconstitution data, but they do not by themselves establish the magnitude of the effect in intact primary B cells. (nocka2023stimulationofthe pages 4-6)
GRB2 participates in B-cell-receptor signalosomes, lymphocyte differentiation, B-cell maturation, T-cell activation, and actin remodeling during phagocytosis. Reported partners include BCAP, Gab proteins, and HPK1. In this setting, GRB2’s core role remains the same: it recruits enzymes and scaffolds to phosphorylated receptors or membrane-associated assemblies rather than providing catalytic activity itself. (malagrino2024grb2adynamic pages 3-3)
GRB2 recognizes FAK Tyr925 and links integrin/FAK signaling to MAPK and motility programs. Direct imaging further shows that EGF-activated EGFR, GRB2, Src, and β5-integrin are captured in plasma-membrane clathrin structures. In human HSC3 cells, EGF drove remodeling into enlarged flat clathrin plaques that integrated growth-factor and adhesion signals. Across four cells, flat structures increased from 141 at baseline to 559 at 15 minutes; dome and spherical structures changed from 46/68 to 67/207. These measurements demonstrate spatial integration at the membrane, although they do not establish direct GRB2–clathrin binding. (wang2024theconfigurationof pages 12-14, alfonzomendez2022dualclathrinand pages 1-3)
GRB2 is also part of receptor downregulation. In receptor-mutant, RNA-interference, and dominant-negative experiments, eliminating EGFR Tyr1068/Tyr1086 GRB2-binding sites, depleting GRB2, or disrupting GRB2 SH3 function impaired entry of EGFR into clathrin-coated pits. GRB2 recruits Cbl, facilitating receptor-associated ubiquitylation and internalization. Thus, GRB2 can both initiate downstream RAS signaling and help terminate or reshape the signal through endocytosis and lysosomal routing. (wang2024theconfigurationof pages 9-11, jiang2003grb2regulatesinternalization pages 1-2)
GRB2 is a soluble intracellular protein found predominantly in the cytoplasm under basal conditions, but its localization is highly dynamic:
GRB2 therefore acts inside the cell, chiefly at the cytoplasmic face of activated membranes and in intracellular protein assemblies; it is not a secreted or transmembrane protein.
GRB2 function is governed by ligand availability, phosphorylation of binding partners, competition among ligands, interdomain coupling, and post-translational modification. Examples include FGFR2-dependent GRB2 Tyr209 phosphorylation and RBBP6-dependent ubiquitination of GRB2 Lys109 during DNA-damage-complex disassembly. Possible dimerization has been reported, and dual SHC phosphorylation may favor recruitment of dimeric GRB2, but dimerization is not required for every mechanism: the 2023 BTK study found no measurable GRB2-induced increase in BTK dimer abundance. (wang2024theconfigurationof pages 12-14, wang2024theconfigurationof pages 11-12, nocka2023stimulationofthe pages 11-13, wang2024theconfigurationof pages 4-5)
Nocka and colleagues showed directly that GRB2 is more than a passive tether in BTK signaling: it binds membrane-associated BTK, relieves an autoinhibited configuration, and increases substrate phosphorylation. This expands the functional concept of an adaptor from simple recruitment to allosteric control of a partner enzyme. DOI: https://doi.org/10.7554/eLife.82676. (nocka2023stimulationofthe pages 11-13, nocka2023stimulationofthe pages 1-2)
Qiu and colleagues reported that oncogenic CCDC6–RET recruits GRB2 and SHC1 into cytoplasmic condensate-like granules in transfected HEK293T cells. Deleting the GRB2 SH2 domain almost abolished granules and signaling; kinase-defective CCDC6–RET K147M and phase-separation-defective Δ21–27 also failed to form the niche. RET inhibitors LOXO292 and BLU667 at 1 µM reduced signaling and interactions, while vandetanib at 5 µM produced partial blockade. Imaging sampled three regions containing more than 200 cells each, with at least three replicates and effects reaching P < 0.0001. DOI: https://doi.org/10.1073/pnas.2322359121. (qiu2024ccdc6retfusionprotein pages 7-8, qiu2024ccdc6retfusionprotein pages 8-9, qiu2024ccdc6retfusionprotein pages 6-7)
This study supports a model in which GRB2 helps concentrate oncogenic signaling, but its limitations are important: the evidence came largely from transfected HEK293T cells, tagged proteins, and overexpression; a purified three-component phase-separation reconstruction and definitive in-vivo validation were not shown in the retrieved evidence. (qiu2024ccdc6retfusionprotein pages 7-8, qiu2024ccdc6retfusionprotein pages 8-9)
Two 2024 reviews emphasize GRB2 as a dynamic, conformationally coupled interaction hub rather than a rigid connector. They highlight domain-specific binding energetics, interfaces between domains, and allosteric sites as possible intervention points. These are authoritative syntheses, not demonstrations that a GRB2-directed drug has achieved clinical efficacy. DOI: https://doi.org/10.3390/biom14030259, published 22 February 2024; DOI: https://doi.org/10.1016/j.bbrep.2024.101803, accepted 26 July and published September 2024. (wang2024theconfigurationof pages 1-2, malagrino2024grb2adynamic pages 2-3, malagrino2024grb2adynamic pages 1-2)
GRB2 is most compelling as a network dependency rather than a frequently mutated oncogenic enzyme. Open Targets associates human GRB2 with cancer, melanoma, chronic myeloid leukemia, bone-development disorders, and listeriosis, but such association scores aggregate heterogeneous genetic, expression, pathway, and literature evidence; they do not demonstrate that GRB2 is independently causal or clinically validated as a drug target. For the broad “cancer” category, GRB2 had an association score of approximately 0.688 in the retrieved Open Targets result. (OpenTargets Search: -GRB2)
Current practical applications include:
The strongest functional annotation is: GRB2 is a phosphorylation-responsive adaptor that assembles receptor-proximal signaling and trafficking complexes, principally coupling activated RTKs to SOS–RAS–MAPK. This conclusion is supported by decades of receptor mutagenesis, structural biology, biochemical binding studies, live-cell imaging, and recent membrane reconstitution. Its endocytic role is also strongly supported by loss-of-function and receptor-site-mutant experiments. (wang2024theconfigurationof pages 1-2, wang2024theconfigurationof pages 9-11, jiang2003grb2regulatesinternalization pages 1-2)
The PI3K–AKT, immune, cytoskeletal, and nuclear roles are biologically plausible extensions of the same modular interaction logic, but they differ in evidentiary maturity. Gab-mediated PI3K coupling and immune signaling have substantial literature support; the specific nuclear functions remain comparatively uncertain. Likewise, condensate-based signaling is an important emerging framework, but current CCDC6–RET evidence should not yet be generalized to every GRB2-containing complex or interpreted as clinical validation of phase-separation-directed therapy. (wang2024theconfigurationof pages 2-4, malagrino2024grb2adynamic pages 3-3, qiu2024ccdc6retfusionprotein pages 7-8, wang2024theconfigurationof pages 4-5)
| Aspect/pathway | Molecular interaction or location | Functional consequence | Strongest evidence/type | Key quantitative detail |
|---|---|---|---|---|
| Canonical RTK–SOS–RAS/MAPK | Plasma-membrane RTK phosphotyrosines recruit the GRB2 SH2 domain; GRB2 SH3 domains bind proline-rich SOS, placing its Ras-GEF activity near membrane-bound Ras | Converts receptor phosphorylation into Ras-GTP loading and RAF–MEK–ERK signaling governing proliferation, survival, and differentiation | Structural, biochemical, mutagenesis, and cell-signaling evidence synthesized in 2024 reviews; EGFR Tyr1068 is a principal GRB2 site and Tyr1086 a secondary site (wang2024theconfigurationof pages 1-2, wang2024theconfigurationof pages 9-11, malagrino2024grb2adynamic pages 2-3) | Human GRB2 is a 217-aa, approximately 25-kDa adaptor; central SH2 spans residues 60–152 in the cited annotation, and the full-length crystal structure was solved at 3.1 Å (wang2024theconfigurationof pages 1-2, malagrino2024grb2adynamic pages 2-3) |
| Gab1–PI3K/AKT | GRB2 C-terminal SH3 domain binds the proline-rich docking protein Gab1 downstream of activated RTKs | Recruits a signaling scaffold that couples receptors to PI3K–AKT survival signaling; this is parallel to, rather than identical with, the SOS–RAS branch | Interaction/pathway synthesis in a 2024 GRB2 review; evidence base includes domain-binding and signaling studies (wang2024theconfigurationof pages 2-4, malagrino2024grb2adynamic pages 3-3) | No robust affinity or pathway-effect size was available in the retrieved evidence; C-SH3 preference was reported as P-X-X-R-X-X-K-P (malagrino2024grb2adynamic pages 2-3) |
| BTK–PLCγ2 signaling | At PIP3-containing membranes, GRB2 binds BTK’s 44-residue, proline-rich linker through its SH3 domains while leaving phosphotyrosine binding by the SH2 domain dispensable | Relieves BTK autoinhibition, recruits BTK into LAT signaling clusters, and accelerates phosphorylation of a PLCγ2 segment | Direct 2023 supported-lipid-bilayer reconstitution, TIRF imaging, construct deletion analysis, and kinase assays; intact full-length GRB2 was required (nocka2023stimulationofthe pages 11-13, nocka2023stimulationofthe pages 4-6, nocka2023stimulationofthe pages 1-2) | Bilayers contained 4% PIP3 or, in tethering assays, 4% DGS-NTA(Ni); fluorescent GRB2 labeling was approximately 17%. GRB2 did not measurably increase BTK dimer abundance (nocka2023stimulationofthe pages 11-13, nocka2023stimulationofthe pages 4-6) |
| EGFR endocytosis | GRB2 binds activated EGFR at Tyr1068/Tyr1086, recruits Cbl, and links receptor complexes to clathrin-coated pits and endocytic machinery | Promotes EGFR ubiquitylation, entry into coated pits, internalization, endosomal trafficking, and eventual signal attenuation/degradation | Direct receptor-mutant, GRB2-RNAi, dominant-negative SH3-mutant, colocalization, and internalization experiments in PAE and human HeLa cells (wang2024theconfigurationof pages 9-11, jiang2003grb2regulatesinternalization pages 1-2) | Simultaneous EGFR Y1068/Y1086 mutation abolished GRB2-dependent internalization in the cited experiments; retrieved excerpts did not provide a numerical internalization rate (jiang2003grb2regulatesinternalization pages 1-2) |
| Integrin/clathrin spatial signaling | EGF-activated EGFR, GRB2, Src, and β5-integrin are captured at plasma-membrane clathrin structures, which enlarge into flat signaling plaques | Spatially integrates growth-factor, adhesion, and endocytic signals and enhances EGFR–Src–integrin crosstalk | Direct quantitative fluorescence and platinum-replica electron microscopy in human HSC3 cells, including genome-edited endogenous EGFR–GFP (alfonzomendez2022dualclathrinand pages 1-3) | Across four cells, flat clathrin structures increased from 141 at 0 min to 559 at 15 min after EGF; corresponding dome/sphere counts were 46/68 and 67/207 (alfonzomendez2022dualclathrinand pages 1-3) |
| Nuclear DNA-damage response | Nuclear GRB2 binds phosphorylated H2AX through its SH2 domain, associates with PTEN/Rad51-related machinery, and recruits an MRE11-containing complex to DNA double-strand breaks; RBBP6-dependent K109 ubiquitination promotes complex dissociation | Proposed scaffolding role in damage-site assembly and homologous-recombination-associated responses, distinct from the canonical membrane pathway | Cell/tissue localization and interaction studies summarized in a 2024 review; authors caution that nuclear localization and function remain incompletely resolved (wang2024theconfigurationof pages 4-5) | Reported nuclear GRB2 staining was 58% in breast tumor tissue versus 22% in normal breast tissue; in NIH-3T3 cells, 30 min of EGF drove nuclear exit and increased Shc interaction (wang2024theconfigurationof pages 4-5) |
| CCDC6–RET oncogenic condensates (2024) | In transfected human HEK293T cells, CCDC6–RET recruits GRB2 and SHC1 into cytoplasmic granules/condensate-like signaling niches; recruitment depends strongly on the GRB2 SH2 domain and fusion kinase/phase-separation competence | Concentrates signaling components and sustains Ras/MAPK activation; RET inhibitors disrupt interactions and signaling, suggesting a pharmacologically tractable oncogenic assembly | Direct live-cell imaging, optogenetic clustering, reciprocal co-immunoprecipitation, domain/point mutants, immunoblotting, and inhibitor perturbation in a 2024 PNAS study (qiu2024ccdc6retfusionprotein pages 7-8, qiu2024ccdc6retfusionprotein pages 8-9, qiu2024ccdc6retfusionprotein pages 6-7) | Imaging sampled three regions containing more than 200 cells each with at least three replicates; effects reached P < 0.0001. LOXO292 and BLU667 were tested at 1 µM and vandetanib at 5 µM; the system relied on transfection/overexpression and was not purified-protein or in-vivo validation (qiu2024ccdc6retfusionprotein pages 7-8, qiu2024ccdc6retfusionprotein pages 8-9) |
Table: Compact evidence map linking human GRB2 (P62993) interactions and cellular locations to functional outcomes. It separates established mechanisms from emerging condensate and nuclear findings while retaining key quantitative details and evidence types.
Human GRB2/P62993 is a conserved, non-enzymatic SH3–SH2–SH3 adaptor whose primary role is to translate receptor and scaffold phosphorylation into localized multiprotein assemblies. At the plasma membrane it recruits SOS to activate RAS–MAPK; through Gab proteins it supports PI3K–AKT; in immune membranes it can activate and cluster BTK, enabling PLCγ2 signaling; and in clathrin-associated structures it couples receptor signaling to internalization. Emerging 2023–2024 research shows that GRB2 can allosterically activate partner enzymes and organize oncogenic condensate-like niches. These advances strengthen GRB2’s value as a mechanistic biomarker and interaction-network target, while also highlighting the principal translational obstacle: GRB2 is a ubiquitous hub whose direct systemic inhibition may disrupt essential normal signaling.
References
(OpenTargets Search: -GRB2): Open Targets Query (-GRB2, 37 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.
(wang2024theconfigurationof pages 1-2): Dingyi Wang, Guoxia Liu, Yuxin Meng, Hongjie Chen, Zu Ye, and Ji Jing. The configuration of grb2 in protein interaction and signal transduction. Biomolecules, 14:259, Feb 2024. URL: https://doi.org/10.3390/biom14030259, doi:10.3390/biom14030259. This article has 67 citations.
(nocka2023stimulationofthe pages 11-13): LM Nocka, TJ Eisen, AT Iavarone, JT Groves, and J Kuriyan. Stimulation of the catalytic activity of the tyrosine kinase btk by the adaptor protein grb2. eLife, Aug 2023. URL: https://doi.org/10.7554/elife.82676, doi:10.7554/elife.82676. This article has 14 citations and is from a domain leading peer-reviewed journal.
(wang2024theconfigurationof pages 2-4): Dingyi Wang, Guoxia Liu, Yuxin Meng, Hongjie Chen, Zu Ye, and Ji Jing. The configuration of grb2 in protein interaction and signal transduction. Biomolecules, 14:259, Feb 2024. URL: https://doi.org/10.3390/biom14030259, doi:10.3390/biom14030259. This article has 67 citations.
(qiu2024ccdc6retfusionprotein pages 8-9): Ting Qiu, Yichao Kong, Guifeng Wei, Kai Sun, Ruijie Wang, Yang Wang, Yiji Chen, Wenxin Wang, Yun Zhang, Caihong Jiang, Peiguo Yang, Tian Xie, and Xiabin Chen. Ccdc6-ret fusion protein regulates ras/mapk signaling through the fusion- grb2-shc1 signal niche. Proceedings of the National Academy of Sciences of the United States of America, May 2024. URL: https://doi.org/10.1073/pnas.2322359121, doi:10.1073/pnas.2322359121. This article has 26 citations and is from a highest quality peer-reviewed journal.
(malagrino2024grb2adynamic pages 2-3): Francesca Malagrinò, Elena Puglisi, Livia Pagano, Carlo Travaglini-Allocatelli, and Angelo Toto. Grb2: a dynamic adaptor protein orchestrating cellular signaling in health and disease. Sep 2024. URL: https://doi.org/10.1016/j.bbrep.2024.101803, doi:10.1016/j.bbrep.2024.101803. This article has 27 citations and is from a peer-reviewed journal.
(wang2024theconfigurationof pages 12-14): Dingyi Wang, Guoxia Liu, Yuxin Meng, Hongjie Chen, Zu Ye, and Ji Jing. The configuration of grb2 in protein interaction and signal transduction. Biomolecules, 14:259, Feb 2024. URL: https://doi.org/10.3390/biom14030259, doi:10.3390/biom14030259. This article has 67 citations.
(wang2024theconfigurationof pages 9-11): Dingyi Wang, Guoxia Liu, Yuxin Meng, Hongjie Chen, Zu Ye, and Ji Jing. The configuration of grb2 in protein interaction and signal transduction. Biomolecules, 14:259, Feb 2024. URL: https://doi.org/10.3390/biom14030259, doi:10.3390/biom14030259. This article has 67 citations.
(malagrino2024grb2adynamic pages 1-2): Francesca Malagrinò, Elena Puglisi, Livia Pagano, Carlo Travaglini-Allocatelli, and Angelo Toto. Grb2: a dynamic adaptor protein orchestrating cellular signaling in health and disease. Sep 2024. URL: https://doi.org/10.1016/j.bbrep.2024.101803, doi:10.1016/j.bbrep.2024.101803. This article has 27 citations and is from a peer-reviewed journal.
(malagrino2024grb2adynamic pages 3-3): Francesca Malagrinò, Elena Puglisi, Livia Pagano, Carlo Travaglini-Allocatelli, and Angelo Toto. Grb2: a dynamic adaptor protein orchestrating cellular signaling in health and disease. Sep 2024. URL: https://doi.org/10.1016/j.bbrep.2024.101803, doi:10.1016/j.bbrep.2024.101803. This article has 27 citations and is from a peer-reviewed journal.
(wang2024theconfigurationof pages 11-12): Dingyi Wang, Guoxia Liu, Yuxin Meng, Hongjie Chen, Zu Ye, and Ji Jing. The configuration of grb2 in protein interaction and signal transduction. Biomolecules, 14:259, Feb 2024. URL: https://doi.org/10.3390/biom14030259, doi:10.3390/biom14030259. This article has 67 citations.
(nocka2023stimulationofthe pages 1-2): LM Nocka, TJ Eisen, AT Iavarone, JT Groves, and J Kuriyan. Stimulation of the catalytic activity of the tyrosine kinase btk by the adaptor protein grb2. eLife, Aug 2023. URL: https://doi.org/10.7554/elife.82676, doi:10.7554/elife.82676. This article has 14 citations and is from a domain leading peer-reviewed journal.
(nocka2023stimulationofthe pages 4-6): LM Nocka, TJ Eisen, AT Iavarone, JT Groves, and J Kuriyan. Stimulation of the catalytic activity of the tyrosine kinase btk by the adaptor protein grb2. eLife, Aug 2023. URL: https://doi.org/10.7554/elife.82676, doi:10.7554/elife.82676. This article has 14 citations and is from a domain leading peer-reviewed journal.
(alfonzomendez2022dualclathrinand pages 1-3): Marco A. Alfonzo-Méndez, Kem A. Sochacki, Marie-Paule Strub, and Justin W. Taraska. Dual clathrin and integrin signaling systems regulate growth factor receptor activation. Nature Communications, Feb 2022. URL: https://doi.org/10.1038/s41467-022-28373-x, doi:10.1038/s41467-022-28373-x. This article has 61 citations and is from a highest quality peer-reviewed journal.
(jiang2003grb2regulatesinternalization pages 1-2): Xuejun Jiang, Fangtian Huang, Andriy Marusyk, and Alexander Sorkin. Grb2 regulates internalization of egf receptors through clathrin-coated pits. Molecular biology of the cell, 14 3:858-70, Mar 2003. URL: https://doi.org/10.1091/mbc.e02-08-0532, doi:10.1091/mbc.e02-08-0532. This article has 411 citations and is from a domain leading peer-reviewed journal.
(wang2024theconfigurationof pages 4-5): Dingyi Wang, Guoxia Liu, Yuxin Meng, Hongjie Chen, Zu Ye, and Ji Jing. The configuration of grb2 in protein interaction and signal transduction. Biomolecules, 14:259, Feb 2024. URL: https://doi.org/10.3390/biom14030259, doi:10.3390/biom14030259. This article has 67 citations.
(qiu2024ccdc6retfusionprotein pages 6-7): Ting Qiu, Yichao Kong, Guifeng Wei, Kai Sun, Ruijie Wang, Yang Wang, Yiji Chen, Wenxin Wang, Yun Zhang, Caihong Jiang, Peiguo Yang, Tian Xie, and Xiabin Chen. Ccdc6-ret fusion protein regulates ras/mapk signaling through the fusion- grb2-shc1 signal niche. Proceedings of the National Academy of Sciences of the United States of America, May 2024. URL: https://doi.org/10.1073/pnas.2322359121, doi:10.1073/pnas.2322359121. This article has 26 citations and is from a highest quality peer-reviewed journal.
(qiu2024ccdc6retfusionprotein pages 7-8): Ting Qiu, Yichao Kong, Guifeng Wei, Kai Sun, Ruijie Wang, Yang Wang, Yiji Chen, Wenxin Wang, Yun Zhang, Caihong Jiang, Peiguo Yang, Tian Xie, and Xiabin Chen. Ccdc6-ret fusion protein regulates ras/mapk signaling through the fusion- grb2-shc1 signal niche. Proceedings of the National Academy of Sciences of the United States of America, May 2024. URL: https://doi.org/10.1073/pnas.2322359121, doi:10.1073/pnas.2322359121. This article has 26 citations and is from a highest quality peer-reviewed journal.
(wang2024theconfigurationof pages 19-21): Dingyi Wang, Guoxia Liu, Yuxin Meng, Hongjie Chen, Zu Ye, and Ji Jing. The configuration of grb2 in protein interaction and signal transduction. Biomolecules, 14:259, Feb 2024. URL: https://doi.org/10.3390/biom14030259, doi:10.3390/biom14030259. This article has 67 citations.