| 2003 |
Fyn is required for Reelin-induced tyrosine phosphorylation and downregulation of the adaptor protein Disabled-1 (Dab1) in neurons. Fyn directly phosphorylates Dab1, and genetic reduction of Fyn copy number reduces Dab1 phosphorylation stoichiometry in vivo; Src partially compensates when Fyn is reduced, but Yes does not. |
Pharmacological Src-family kinase inhibition, analysis of Dab1 phosphorylation in fyn/src/yes mutant mouse embryos, cultured neuron assays |
Current biology : CB |
High |
12526739
|
| 2005 |
Combined absence of Src and Fyn nearly abolishes Dab1 tyrosine phosphorylation and phenocopies the reeler phenotype (inverted cortical layering, impaired Purkinje plate formation), demonstrating that Src and Fyn are the principal kinases mediating Reelin-dependent neuronal migration in vivo. |
Double Src/Fyn knockout mice, immunohistochemistry, Dab1 phosphorylation biochemistry |
The Journal of neuroscience : the official journal of the Society for Neuroscience |
High |
16162939
|
| 2002 |
FcεRI activation of mast cells engages a Fyn kinase-dependent signaling pathway that is distinct from the Lyn/LAT pathway and is specifically required for mast cell degranulation. Fyn deficiency impairs degranulation while leaving the calcium response intact; Lyn deficiency enhances Fyn-dependent signals. |
Fyn-knockout and Lyn-knockout mast cells, degranulation assays, calcium measurement |
Nature immunology |
High |
12089510
|
| 2003 |
Fyn directly binds Nephrin via its SH3 domain and phosphorylates Nephrin on tyrosine in podocyte lipid-raft membrane fractions. Genetic deletion of Fyn in mice causes coarsening of podocyte foot processes and markedly reduces Nephrin phosphorylation in glomerular detergent-resistant membrane fractions. |
Biochemical fractionation, direct binding assays (SH3-domain pulldown), in vitro kinase assay, Fyn/Yes knockout mice, glomerular morphology analysis |
The Journal of biological chemistry |
High |
12668668
|
| 2004 |
Fyn phosphorylates the cytoplasmic domain of Nephrin on multiple tyrosine residues more potently than Src. This phosphorylation augments the interaction between Nephrin and Podocin and activates AP-1 promoter signaling downstream of Nephrin/Podocin. |
Co-transfection of Cos-1 cells, tyrosine-to-phenylalanine mutagenesis, co-immunoprecipitation, AP-1 reporter assay |
Journal of the American Society of Nephrology : JASN |
High |
15579503
|
| 2006 |
Coxsackievirus attachment to DAF on the apical epithelial surface activates Fyn kinase, which is required for phosphorylation of caveolin and transport of the virus into the cell within caveolar vesicles. |
Inhibitor studies, siRNA, caveolar transport assays in polarized epithelial cells |
Cell |
High |
16413486
|
| 1995 |
Fyn participates in regulation of focal adhesion kinase (FAK) and paxillin phosphorylation in the cytoskeleton downstream of Csk. Double-mutant genetic analysis shows Fyn and Src have overlapping but distinct roles: Src controls cortactin and tensin phosphorylation, while FAK/paxillin phosphorylation is partly dependent on both. |
Genetic epistasis in src/fyn/csk triple-mutant mouse embryos, tyrosine phosphorylation biochemistry, immunofluorescence of actin and cortactin |
Nature |
High |
7617039
|
| 1995 |
Fyn kinase is activated in mouse keratinocytes during calcium- or TPA-induced differentiation, phosphorylates cortactin (p80-85), and is specifically required for keratinocyte differentiation; fyn-null keratinocytes show no p80-85 phosphorylation induction and are impaired in differentiation both in vitro and in vivo. |
Kinase activity immunoprecipitation assay, fyn/yes knockout keratinocytes, in vitro and in vivo differentiation assays |
Genes & development |
High |
7557381
|
| 1999 |
Fyn mediates reactive oxygen species (H2O2)-induced activation of JAK2, leading to Shc tyrosine phosphorylation and Ras activation. This pathway is Fyn-specific: H2O2-stimulated JAK2, Shc, and Ras activation are abolished in Fyn-/- fibroblasts but unaltered in Src-/- fibroblasts; re-expression of Fyn (but not Src) rescues JAK2 activation. |
Fyn-/- and Src-/- fibroblasts, kinase activity assays, Ras-GTP pull-down, rescue by transfection of Fyn vs. Src |
The Journal of biological chemistry |
High |
10409649
|
| 2000 |
PKC-eta directly associates with Fyn and directly activates Fyn kinase activity in vitro. PKC-eta-driven growth suppression of keratinocytes depends on Fyn, placing Fyn downstream of PKC-eta in the keratinocyte growth-arrest/differentiation pathway. Fyn activation alone suppresses keratinocyte (but not fibroblast) growth by downmodulating EGF receptor signaling. |
Co-immunoprecipitation of PKC-eta and Fyn, in vitro kinase assay with recombinant PKC-eta, fyn-KO keratinocytes, EGFR signaling analysis |
Molecular cell |
High |
11106751
|
| 2009 |
Fyn kinase regulates endocytosis of flotillin-1 and flotillin-2: EGF induces flotillin internalization via Fyn (but not Src or Yes) by directly phosphorylating Tyr160 on flotillin-1 and Tyr163 on flotillin-2; mutation of these residues to phenylalanine blocks Fyn-induced flotillin internalization and reduces uptake of the GPI-linked protein CD59. |
SYF cells (Src/Yes/Fyn-null) with individual kinase re-expression, rapamycin-inducible Fyn activation system, site-directed mutagenesis (Y→F), GPI-protein endocytosis assay |
Journal of cell science |
High |
19258392
|
| 2006 |
Cell rigidity response on fibronectin requires Fyn (but not endogenous c-Src) at the leading edge. Fyn recruitment depends on its palmitoylation site; adding that palmitoylation site to c-Src enables it to support the rigidity response. Fyn phosphorylates p130Cas at the leading edge in a rigidity-dependent manner. |
Live-cell imaging of GFP-tagged Src-family kinases, palmitoylation-site chimeras, p130Cas phosphorylation assay at leading edges |
Molecular biology of the cell |
Medium |
16597701
|
| 2003 |
Integrin αvβ6 ligation by fibronectin in oral squamous cell carcinoma forms a complex with Fyn, activates Fyn kinase, recruits and activates FAK, activates Shc, and couples to the Raf-ERK/MAPK pathway, leading to MMP-3 transcription and promoting cancer cell proliferation and experimental metastasis. |
Co-immunoprecipitation of β6/Fyn/FAK complex, kinase activity assays, MMP-3 reporter, in vivo metastasis model |
The Journal of biological chemistry |
Medium |
12917446
|
| 2000 |
TCR antagonist stimulation selectively activates Fyn kinase and induces Vav tyrosine phosphorylation in a Fyn-dependent manner, without activating Lck or ZAP-70. Fyn-deficient T cells fail to phosphorylate/activate Vav and cannot form APC-T cell conjugates (immunologic synapse) in response to either agonist or antagonist peptides. |
Fyn-/- TCR-transgenic mice, Jurkat cells with differential Lck/Fyn expression, kinase activity assays, Vav phosphorylation, conjugate formation assay |
Proceedings of the National Academy of Sciences of the United States of America |
High |
11005864
|
| 1998 |
Fyn is N-myristoylated on cytosolic polysomes and then targeted to the plasma membrane where it is palmitoylated. Dual acylation clusters Fyn in caveolae-like membrane microdomains. |
Biochemical acylation analysis, membrane fractionation, lipid raft/caveolae isolation (review with primary biochemical data cited) |
The international journal of biochemistry & cell biology |
Medium |
9839441
|
| 1998 |
CD73 ligation-mediated signal transduction in murine T lymphocytes requires Fyn kinase: fyn-/- mice are unresponsive to CD73-mediated signaling, demonstrating a necessary role for Fyn in this GPI-anchored protein signaling pathway. |
fyn-/- mice, anti-CD73 mAb stimulation, T cell proliferation and IL-2 secretion assays |
European journal of immunology |
Medium |
9808167
|
| 2005 |
Receptor protein tyrosine phosphatase alpha (PTPα) suppresses Fyn activity in thymocyte lipid rafts. In PTPα-/- thymocytes, raft-associated Fyn is hyperactivated due to increased phosphorylation at its activating (Tyr417) and inhibitory (Tyr528) residues. Hyperactive Fyn then phosphorylates Cbp/PAG, promoting its association with C-terminal Src kinase (Csk). |
PTPα-knockout thymocytes, lipid raft fractionation, Fyn kinase activity assay, phospho-specific antibodies for Fyn Tyr417/528, Cbp/PAG co-IP with Csk |
Journal of immunology (Baltimore, Md. : 1950) |
High |
16339530
|
| 2015 |
STEP (STriatal-Enriched protein tyrosine Phosphatase) dephosphorylates PTPα at Tyr789, preventing PTPα translocation to synaptic membranes and blocking its ability to activate Fyn. Upon ethanol exposure, PKA phosphorylates and inactivates STEP, allowing PTPα to translocate to lipid rafts and activate Fyn, which then upregulates GluN2B-containing NMDA receptor signaling. |
Primary neuronal cultures, STEP knockdown/pharmacological inhibition, phospho-specific antibodies, synaptosomal fractionation, in vitro phosphatase assay, in vivo ethanol treatment |
Journal of neurochemistry |
High |
25951993
|
| 2009 |
Netrin-1 binding to DCC on mature oligodendrocytes recruits Fyn to a complex with the DCC intracellular domain that includes FAK and N-WASP, resulting in RhoA inhibition and induction of process remodeling. Fyn-/- oligodendrocytes fail to increase process branching in response to netrin-1. |
Fyn-knockout oligodendrocyte cultures, co-immunoprecipitation of DCC/Fyn/FAK/N-WASP complex, RhoA activity assay, in vitro process branching assay, in vivo netrin-1/DCC expression studies |
Development (Cambridge, England) |
High |
19141671
|
| 2016 |
FYN interacts with the C-terminal domain of NOX4, colocalizes with NOX4 in perinuclear mitochondria/ER/nuclear fractions in cardiomyocytes, and directly phosphorylates NOX4 at Tyr566 to negatively regulate NOX4-induced superoxide production and apoptosis. FYN-deficient mice show exacerbated cardiac hypertrophy; Nox4 deletion rescues this phenotype. |
Co-immunoprecipitation, co-localization imaging, site-directed mutagenesis of Tyr566, in vitro kinase assay, Fyn-KO and Nox4-KO mice, transverse aortic constriction model |
The Journal of clinical investigation |
High |
27525436
|
| 2017 |
Fyn phosphorylates SHP-1 at Ser591 (inactivating the phosphatase), enabling activatory immunoreceptor (ITAM) signaling. By contrast, Lyn phosphorylates SHP-1 at Tyr536 (activating the phosphatase), promoting inhibitory signaling. Thus Fyn and Lyn have opposing roles in controlling immunoreceptor signaling status. |
Site-specific phosphorylation assays, SHP-1 mutagenesis, Fyn-/- and Lyn-/- mice, nephritis and arthritis in vivo models |
Nature communications |
High |
28811476
|
| 2015 |
Fyn inhibition (AZD0530) potently inhibits Fyn and prevents Aβ oligomer-induced signaling through Fyn to Pyk2 and NR2B NMDA receptors in brain slices. In APP/PS1 mice, AZD0530 fully rescues spatial memory, synaptic depletion, and reduces microglial activation without affecting Aβ metabolism; it also rescues Tau phosphorylation in APP/PS1/Tau mice. |
Brain slice signaling assays, pharmacokinetics, Morris water maze, novel object recognition, immunohistochemistry, immunoblotting in APP/PS1 and triple-transgenic mice |
Annals of neurology |
High |
25707991
|
| 2019 |
Fyn kinase, in conjunction with CD36, regulates microglial uptake of aggregated α-synuclein. Fyn mediates PKCδ-dependent NF-κB-p65 nuclear translocation leading to NLRP3 inflammasome priming, and facilitates αSyn import into microglia to generate mitochondrial ROS that activate the NLRP3 inflammasome. |
Fyn-KO mice, A53T and viral αSyn overexpression mouse models, siRNA knockdown, NF-κB reporter, NLRP3 inflammasome activation assays, human PD neuropathology |
The Journal of experimental medicine |
High |
31036561
|
| 2018 |
Fyn directly colocalizes with and phosphorylates β-catenin at Tyr142 in articular chondrocytes, stabilizing β-catenin and promoting its nuclear translocation, thereby upregulating catabolic enzymes and accelerating cartilage degradation and osteoarthritis development. |
Co-immunoprecipitation, phosphorylation assay with Tyr142 site-specific analysis, Fyn-KO mice with destabilization-of-medial-meniscus OA model, pharmacological Fyn inhibition (AZD0530, PP1) |
Annals of the rheumatic diseases |
High |
29555825
|
| 2020 |
Fyn kinase controls tau aggregation in vivo independently of Aβ. Fyn-knockout in a mutant-tau transgenic mouse (Tg/Fyn-/-) nearly abolishes neurofibrillary tangles, reduces tau hyperphosphorylation, alters tau solubility, diminishes synaptic tau accumulation, and reduces tau seeding capacity. Pseudophosphorylation of tau at the Fyn epitope Y18 boosts tau fibrillization in vitro. |
Fyn-KO crossed to tau-transgenic mice, tau seeding biosensor assay, in vitro fibrillization assay with phosphomimetic tau Y18E |
Cell reports |
High |
32814048
|
| 2018 |
Pyk2 is a novel tau tyrosine kinase that colocalizes, interacts with, and phosphorylates tau in vivo and in vitro. Pyk2 activity is increased in Fyn-constitutively-active mice and decreased in Fyn-KO mice, placing Pyk2 as a direct tau kinase acting downstream of Fyn. |
Pyk2-transgenic and Pyk2/tau double-transgenic mice, in vitro kinase assay of Pyk2 phosphorylating tau, co-immunoprecipitation, FynCA and FynKO mice |
Journal of Alzheimer's disease : JAD |
Medium |
29782321
|
| 2006 |
Fyn mediates transactivation of Trk receptor tyrosine kinases by adenosine (a G-protein-coupled receptor ligand). Fyn and Trk colocalize in a juxtanuclear membrane compartment, adenosine activates Fyn, and Fyn directly phosphorylates Trk in vitro with kinetics matching Trk activation in cells. |
Co-localization imaging, in vitro Fyn phosphorylation of Trk assay, adenosine stimulation time-course, Fyn overexpression rescue |
Molecular and cellular neurosciences |
Medium |
16860569
|
| 2015 |
BDNF activation of oligodendroglial TrkB receptors stimulates Fyn phosphorylation, which is necessary for subsequent phosphorylation of Erk1/2 and promotion of CNS myelination. A kinase-dead Fyn mutant inhibits BDNF-induced Erk1/2 activation and abrogates BDNF's promyelinating effect. |
Myelinating cocultures, PP2 inhibitor, kinase-dead Fyn overexpression, Fyn overexpression in oligodendrocytes, in vivo Fyn phosphorylation co-localization with mature oligodendrocytes |
Glia |
Medium |
26449489
|
| 2015 |
Tyro3 receptor tyrosine kinase binds Fyn via affinity chromatography of the Tyro3 intracellular domain, and Fyn kinase activity is downregulated in Tyro3-KO mice. Fyn-KO mice exhibit reduced myelin thickness and decreased myelination in Schwann cell-neuron cocultures, identifying Tyro3-Fyn as a receptor-linked signaling mechanism controlling Schwann cell myelination. |
Affinity chromatography to identify Fyn as Tyro3 binding partner, Tyro3-KO and Fyn-KO mice, dorsal root ganglion cocultures, myelin thickness measurement |
Molecular biology of the cell |
Medium |
26224309
|
| 2011 |
Fyn regulates apoptosis in pancreatic cancer by controlling HnRNPA2B1 and Sam68: Fyn activity maintains HnRNPA2B1 expression (which promotes anti-apoptotic Bcl-xL splicing via blocking Bcl-xS formation) and phosphorylates Sam68 (reducing its pro-Bcl-xL splicing activity). Loss of Fyn kinase activity reduces HnRNPA2B1 and decreases Sam68 phosphorylation, shifting Bcl-x splicing toward the pro-apoptotic Bcl-xS. |
Kinase-dead Fyn transfection, HnRNPA2B1 siRNA, Sam68 siRNA, Bcl-x splicing assay, apoptosis assays |
Carcinogenesis |
Medium |
21642356
|
| 2011 |
Fyn mediates hyperosmolarity-induced retrieval of the bile canalicular transporters Mrp2 and Bsep from the canalicular membrane in rat liver. This is driven by NADPH oxidase-generated ROS activating Fyn. Fyn associates with cortactin and increases cortactin phosphorylation beneath the canalicular membrane, contributing to transporter retrieval. |
Perfused rat liver model, Fyn-specific inhibitor PP-2, Fyn siRNA knockdown, p47phox-KO mice, co-immunoprecipitation of Fyn-cortactin, cortactin phosphorylation assay, biliary excretion measurement |
The Journal of biological chemistry |
Medium |
22057277
|
| 2016 |
FYN associates with FLT3 (both wild-type and oncogenic FLT3-ITD) via the FYN SH2 domain interacting with multiple FLT3 phosphotyrosine sites in a kinase-activity-dependent manner. FYN expression selectively potentiates FLT3-ITD-dependent STAT5 phosphorylation and colony formation. |
Co-immunoprecipitation, SH2-domain mutant FYN, FYN overexpression in FLT3-ITD cells, phospho-STAT5/AKT/ERK immunoblotting, colony formation assay |
Oncotarget |
Medium |
26848862
|
| 2012 |
IFNγ induces Fyn-dependent phosphorylation of E-cadherin and p120-catenin, leading to E-cadherin internalization, ubiquitinylation (via Hakai E3 ligase), and proteasomal degradation. Fyn siRNA or the Src-kinase inhibitor PP1 prevents IFNγ-induced E-cadherin internalization and subsequent epithelial barrier disruption. |
siRNA knockdown of Fyn, immunoprecipitation, immunofluorescence confocal microscopy, E-cadherin ubiquitinylation assay, barrier integrity assay |
PloS one |
Medium |
22715382
|
| 2016 |
Fyn deficiency attenuates renal fibrosis through a STAT3-dependent mechanism that is independent of the Smad pathway. STAT3 small interfering RNA in Fyn-deficient cells further suppresses α-SMA expression, and a STAT3 activator partially restores fibrotic markers, placing STAT3 downstream of Fyn in renal fibrogenesis. |
Fyn-KO mice with unilateral ureteral obstruction, pharmacological Fyn inhibition in kidney cell lines, STAT3 siRNA in Fyn-deficient cells, STAT3 activator rescue |
Kidney international |
Medium |
27616741
|
| 2016 |
MOBP (myelin-associated oligodendrocytic basic protein) synthesis is stimulated by Fyn kinase activity in cultured primary oligodendrocytes, and MOBP promotes morphological differentiation of oligodendrocytes. |
Fyn kinase inhibition and activation in primary oligodendrocyte cultures, MOBP expression and morphology analysis |
Journal of cell science |
Low |
26801084
|
| 2015 |
Fyn-phosphorylated PIKE-A binds to and inhibits AMPK's catalytic alpha subunit, impairing T172 phosphorylation and reducing AMPK kinase activity. Fyn depletion or pharmacological Fyn inhibition prevents PIKE-A/AMPK association, restoring AMPK tumor-suppressive activity. |
Co-immunoprecipitation of PIKE-A and AMPK, Fyn phosphorylation-site mutagenesis of PIKE-A, Fyn siRNA/inhibitor, AMPK substrate phosphorylation assay, cell proliferation assay, glioblastoma samples |
Cell death and differentiation |
Medium |
26001218
|
| 2013 |
Fyn regulates adipogenesis by phosphorylating PIKE-A, which then enhances PIKE-A interaction with STAT5a, reducing STAT5a transcriptional activity. Fyn-null or pharmacologically inhibited adipocytes fail to fully differentiate, and PIKE-/- adipose tissue also shows reduced STAT5a activity. |
3T3-L1 adipogenesis model, Fyn-KO cells, Fyn pharmacological inhibition, co-IP of PIKE-A/STAT5a, STAT5a transcriptional reporter |
Molecular and cellular biology |
Medium |
23438599
|
| 2008 |
Lysophosphatidic acid (LPA) induces rapid Fyn activation and increased association of Fyn with p120-catenin at cell-cell junctions in ovarian cancer cells, driving junction dispersal and single-cell migration. This is the principal Src-family kinase recruited to p120-catenin in this context. |
Co-immunoprecipitation of Fyn and p120-catenin after LPA stimulation, PP2 inhibitor, immunofluorescence of junction dynamics |
International journal of cancer |
Low |
18506685
|
| 2014 |
TLR4 physically interacts with Fyn upon LPS stimulation in astrocytes (shown by co-immunoprecipitation and co-localization), and this TLR4-Fyn interaction drives PI3K/Akt/NF-κB-dependent upregulation of PAI-1. Fyn siRNA or PP2 blocks TLR4 tyrosine phosphorylation and LPS-induced PAI-1 expression. |
Co-immunoprecipitation of TLR4-Fyn, immunofluorescence co-localization, Fyn siRNA, PP2 inhibitor, PAI-1 expression assay, neurite outgrowth assay |
Molecular neurobiology |
Medium |
25106729
|
| 2013 |
Fyn kinase is required for dengue virus RNA replication. RNAi depletion of Fyn reduces DV2 RNA replication, and serial passaging of virus under dasatinib or AZD0530 selects a resistance mutation in the NS4B transmembrane domain 3, genetically linking Fyn to the viral RNA replication step. |
RNAi depletion of Src-family kinases, Northern blot and reporter replicon assays, resistance mutation mapping by serial passaging |
Journal of virology |
Medium |
23616652
|
| 2021 |
FYN-TRAF3IP2 is a recurrent oncogenic gene fusion in AITL and PTCL, NOS that drives aberrant NF-κB signaling downstream of T cell receptor activation. Expression of FYN-TRAF3IP2 in hematopoietic progenitors induces NF-κB-driven T cell transformation in mice and cooperates with Tet2 loss in PTCL development; IκB kinase inhibitors suppress FYN-TRAF3IP2-induced lymphoma. |
Identification of fusion by sequencing, hematopoietic progenitor reconstitution mouse model, NF-κB reporter and signaling assays, IKK inhibitor treatment in vitro and in vivo |
Nature cancer |
High |
33928261
|
| 2018 |
Fyn is a modulator of erythropoietin signaling: Fyn-/- mice exhibit reduced tyrosine phosphorylation of EPO-R and decreased STAT5 activity. Fyn also acts as a physiologic repressor of Nrf2; absence of Fyn leads to persistent Nrf2 activation, ROS-induced Jak2-Akt-mTOR pathway overactivation, and impaired autophagy, which can be rescued by rapamycin. |
Fyn-/- mice, EPO-R tyrosine phosphorylation assay, STAT5 activity, Nrf2 target gene expression, mTOR pathway immunoblotting, rapamycin treatment |
American journal of hematology |
Medium |
30252956
|
| 2019 |
Aβ oligomers promote oligodendrocyte differentiation and MBP translation via integrin β1 receptor and Fyn kinase, with Ca2+/CaMKII as downstream effectors. Pharmacological Fyn inhibition attenuates Aβ-induced oligodendrocyte differentiation and MBP upregulation in organotypic cerebellar slices. |
Integrin β1 blockade, Fyn pharmacological inhibition, MBP local translation assay, organotypic cerebellar slice model with lysolecithin demyelination |
Cell death & disease |
Medium |
31171765
|
| 2015 |
P2X7 receptor physically interacts with Fyn kinase (co-immunoprecipitation), and P2X7 receptor agonist BzATP enhances Fyn kinase activity. Blocking Fyn activity or downregulating Fyn expression inhibits BzATP-induced oligodendrocyte progenitor cell migration. |
Co-immunoprecipitation of P2X7 and Fyn, Fyn kinase activity assay, Fyn inhibitor and siRNA knockdown, OPC migration assay |
Purinergic signalling |
Low |
26099359
|
| 2023 |
CD28-containing CAR-T cells signal through FYN kinase rather than LCK for their primary activation. FYN-dependent CAR signaling (requiring both FYN and CD28 intracellular domain) promotes T cell proliferation and memory formation, whereas LCK-dependent signaling leads to exhaustion. LCK-deficient CAR-T cells with intact FYN show superior in vivo anti-tumor efficacy. |
LCK-deficient CAR-T cells, in vivo CAR-T efficacy models, phenotypic analysis of exhaustion/memory markers, CD28 domain mutant CARs |
Cell reports. Medicine |
Medium |
36696897
|
| 2010 |
Fyn kinase localizes to the egg cortex, polar body, fertilizing cone, and meiotic/mitotic spindles of rat eggs. In mammalian oocytes, Fyn concentrates asymmetrically at the site of cleavage furrow ingression co-localizing with F-actin during meiosis and mitosis; dominant-negative Fyn prolongs furrow ingression duration and leads to larger polar bodies and longer spindles. |
Live-cell confocal imaging, microinjection of Fyn cRNA (wild-type and dominant-negative), SFK inhibitor SU6656, polar body extrusion timing and spindle length measurement |
Reproduction (Cambridge, England) |
Medium |
20841362
|
| 2007 |
Fyn phosphorylates APP at Tyr757 of the YENPTY motif and increases APP cell-surface expression. In the presence of Dab1, Fyn significantly increases sAPPα production and C-terminal fragment levels, and potentiates Dab1-dependent APP phosphorylation and surface trafficking. Fyn-KO mice show reduced sAPPα in vivo. |
Co-immunoprecipitation, co-immunostaining, FLIM (fluorescence lifetime imaging), Fyn overexpression with/without Dab1, Fyn-KO mouse brain analysis |
The Journal of biological chemistry |
Medium |
18089558
|
| 2019 |
Fyn kinase activity is regulated by submembrane localization: a FRET biosensor shows that Fyn outside its membrane microdomains is hyperactive, while microdomains provide a suppressive microenvironment. A relatively high Fyn activity is also observed at perinuclear regions. |
FRET biosensor for Fyn kinase activity in live cells, membrane microdomain-targeted biosensor variants (Fyn-tag vs. Lyn-tag), pharmacological perturbations of membrane domains |
ACS sensors |
Medium |
30588803
|