| 1996 |
RSK2 (pp90RSK family) was purified, sequenced, and biochemically characterized as CREB kinase — the kinase that phosphorylates CREB at Ser-133 in response to growth factor-stimulated RAS-MAPK signaling, thereby coupling the RAS-MAPK pathway to immediate early gene transcription. |
Protein purification, sequencing, in vitro kinase assay, in vivo phosphorylation assay |
Science |
High |
8688081
|
| 1996 |
Mutations in RSK2 (Rsk-2 gene) cause Coffin-Lowry syndrome; missense mutations affecting sites critical for RSK2 function render the protein inactive in S6 kinase assays, establishing loss of kinase activity as the disease mechanism. |
Mutation screening, in vitro S6 kinase activity assay |
Nature |
High |
8955270
|
| 1998 |
RSK2 activity is specifically required for EGF-induced CREB Ser-133 phosphorylation and c-fos gene induction; CLS fibroblasts lacking functional RSK2 show dramatically attenuated EGF-stimulated CREB phosphorylation and c-fos expression, restored by wild-type RSK2 re-expression. |
Loss-of-function in CLS patient fibroblasts, transfection rescue, in vivo phosphorylation assay, reporter assay |
Proceedings of the National Academy of Sciences of the United States of America |
High |
9770464
|
| 1999 |
RSK2 is required for EGF-stimulated phosphorylation of histone H3; CLS patient fibroblasts and RSK2-knockout mouse ES cells fail to exhibit EGF-stimulated H3 phosphorylation, while mitotic H3 phosphorylation is unaffected; re-introduction of wild-type RSK2 restores EGF-stimulated H3 phosphorylation. |
Loss-of-function (CLS patient cells and homologous recombination knockout ES cells), rescue by wild-type RSK2 transfection |
Science |
High |
10436156
|
| 1999 |
RSK2 (pp90rsk2) is identical to Fos kinase, which phosphorylates c-Fos at Ser-362 in a RAS/MEK-dependent manner; purified Fos kinase from NGF-stimulated PC12 cells was identified as pp90rsk2 by mass spectrometry and shown to be the same as NGFI-B kinase I. CREB kinase was distinguished as a distinct species from pp90rsk2. |
Affinity purification, mass spectrometry, in vitro kinase assay, chromatographic comparison |
The Journal of biological chemistry |
High |
9920881
|
| 2000 |
Phosphorylation of RSK2 at Ser386 in the hydrophobic motif (by the C-terminal kinase domain) creates a phosphoserine-dependent docking site that recruits PDK1, which then phosphorylates RSK2 at Ser227 (activating the N-terminal kinase domain); a S386K mutant showed no PDK1 interaction or Ser227 phosphorylation; a synthetic pSer386 peptide activated PDK1 6-fold in vitro. |
Co-immunoprecipitation, mutagenesis, in vitro kinase assay with synthetic peptide, in vivo phosphorylation assay |
The EMBO journal |
High |
10856237
|
| 2000 |
Xenopus Rsk2 is the predominant p90Rsk isozyme (~120 nM) in oocytes/eggs, forms a heteromeric complex with p42 MAP kinase via sequences at the extreme C-terminus of Rsk2, and can be activated in vitro by p42 MAP kinase to a specific activity comparable to maximal in vivo activation. |
Protein quantification, co-immunoprecipitation, peptide competition, in vitro kinase reconstitution |
The Journal of biological chemistry |
High |
10934212
|
| 2001 |
RSK2 and CBP form a complex in quiescent cells in which both RSK2 kinase activity and CBP HAT activity are inhibited; mitogenic stimulation causes dissociation dependent on RSK2 Ser227 phosphorylation, releasing both kinase and acetyltransferase activities. |
Co-immunoprecipitation, kinase activity assay, HAT activity assay, mutagenesis (Ser227) |
Molecular and cellular biology |
High |
11564891
|
| 2002 |
RSK2 directly phosphorylates Bad at Ser112 in vitro, and RSK2-deficient CLS cells are defective for UVB-induced Bad Ser112 phosphorylation; phosphorylation of Bad at Ser112 by RSK2 (and JNK1/MSK1) promotes dissociation of Bad from Bcl-XL. |
In vitro kinase assay with active RSK2, RSK2-deficient CLS cells, dominant-negative mutants, co-immunoprecipitation (Bad/Bcl-XL) |
The Journal of biological chemistry |
High |
11983683
|
| 2003 |
PEA-15 binds directly to RSK2 (but not RSK1) via the C-terminus of PEA-15, co-precipitates in cells, blocks RSK2 nuclear accumulation after EGF stimulation, inhibits RSK2 kinase activity by ~50%, and suppresses RSK2-dependent CREB transcription and histone H3 phosphorylation. |
Co-immunoprecipitation from cells, in vitro pulldown with purified PEA-15 and in vitro translated RSK2, kinase assay, reporter assay, nuclear localization assay |
The Journal of biological chemistry |
High |
12796492
|
| 2004 |
ATF4 is a direct substrate of RSK2; RSK2 phosphorylates ATF4 and is required for timely osteoblast differentiation, terminal osteoblast differentiation, osteoblast-specific gene expression, and posttranscriptional regulation of Type I collagen synthesis. ATF4 deficiency recapitulates the skeletal phenotype of CLS. |
In vitro kinase assay, genetic knockout mice (RSK2 and ATF4), osteoblast differentiation assays, gene expression analysis |
Cell |
High |
15109498
|
| 2005 |
RSK2 phosphorylates c-Fos at Ser362, stabilizing c-Fos protein; loss of RSK2 leads to reduced c-Fos levels, decreased proliferation, and increased apoptosis of transformed osteoblasts, impairing c-Fos-dependent osteosarcoma formation in mice. |
RSK2 knockout mice, c-Fos phosphorylation site mutagenesis, osteosarcoma formation assay, apoptosis and proliferation assays |
The Journal of clinical investigation |
High |
15719069
|
| 2007 |
FGFR3 directly tyrosine-phosphorylates RSK2 at Y529, facilitating binding of inactive ERK to RSK2, which is required for ERK-dependent phosphorylation and activation of RSK2; inhibition of RSK2 by siRNA or FMK induces apoptosis in FGFR3-expressing t(4;14)-positive myeloma cells. |
Phospho-proteomics, in vitro kinase assay (FGFR3 + RSK2), co-immunoprecipitation, siRNA knockdown, apoptosis assay |
Cancer cell |
High |
17785202
|
| 2007 |
RSK2 directly interacts with NFAT3 (via both N- and C-terminal kinase domains binding to NLS1/Ser-Pro/polyproline domains of NFAT3), phosphorylates NFAT3 in vitro (Km=3.559 μM), induces NFAT3 nuclear localization upon stimulation, and is required for skeletal muscle cell differentiation into myotubes. |
Co-immunoprecipitation, in vitro kinase assay, RSK2-/- cells, siRNA knockdown, myotube differentiation assay |
The Journal of biological chemistry |
High |
17213202
|
| 2007 |
PEA-15 acts as a scaffold that independently binds ERK and RSK2, increases ERK-RSK2 association in a concentration-dependent manner, enhances RSK2 activity and CREB-mediated transcription, and this scaffolding function is regulated by PEA-15 phosphorylation. PEA-15-null lymphocytes show impaired RSK2 activation rescued by exogenous PEA-15. |
Co-immunoprecipitation, kinase activity assay, reporter assay, PEA-15 knockout lymphocytes, rescue by exogenous PEA-15 |
Proceedings of the National Academy of Sciences of the United States of America |
High |
18077417
|
| 2007 |
EGF-stimulated RSK2 tyrosine phosphorylation at Tyr-529 is mediated by Src family kinases (Src and Fyn), not by EGFR directly; Src/Fyn phosphorylation of Y529 facilitates binding of inactive ERK to RSK2, required for ERK-dependent RSK2 activation; PP2 (Src inhibitor) attenuates EGF-dependent RSK2 activation and Y529 phosphorylation. |
Mass spectrometry identification, in vitro kinase assay (Src/Fyn + recombinant RSK2), GST-RSK2 reconstitution, mutagenesis (Y529F), Src inhibitor PP2 |
The Journal of biological chemistry |
High |
18156174
|
| 2008 |
RSK2 colocalizes with TIA-1 and PABP1 in stress granules in stressed cells; the RSK2 N-terminal kinase domain directly interacts with the prion-related domain of TIA-1; RSK2 sequestration in granules and TIA-1 sequestration are codependent. Upon mitogen stimulation, RSK2 is released from stress granules and translocates to the nucleus via a C-terminal nucleocytoplasmic shuttling sequence, dependent on TIA-1; nuclear RSK2 alone is sufficient to induce cyclin D1 and enhance proliferation. |
Colocalization (fluorescence microscopy), co-immunoprecipitation, domain mapping, siRNA knockdown, nuclear localization assay, cyclin D1 reporter |
Molecular cell |
High |
18775331
|
| 2008 |
RSK2 physically interacts with and phosphorylates PLD1 at Thr-147 in the phox homology domain; expression of inactive RSK2 mutants or RSK2 knockdown dramatically impairs exocytotic response in chromaffin cells; phosphomimetic PLD1-T147 mutant fully restores secretion in RSK2-depleted cells, placing RSK2 upstream of PLD1 in calcium-regulated exocytosis. |
Co-immunoprecipitation, in vitro kinase assay, dominant-negative mutants, siRNA knockdown, phosphomimetic rescue, chromaffin cell exocytosis assay |
Proceedings of the National Academy of Sciences of the United States of America |
High |
18550821
|
| 2009 |
FGFR3 interacts with RSK2 through residue W332 in the RSK2 linker region; this interaction is required for FGFR3-dependent phosphorylation of RSK2 at Y529 and Y707. Phosphorylation at Y707 contributes to RSK2 activation by disrupting the autoinhibitory αL-helix, while Y529 phosphorylation facilitates ERK binding. |
Co-immunoprecipitation, mutagenesis (W332, Y529, Y707), in vitro kinase assay, murine bone marrow transplant with RSK2-knockout cells |
Molecular and cellular biology |
High |
19223461
|
| 2009 |
The RSK2 N-terminal kinase domain (NTD) is required for activation of the ERK-mediated C-terminal kinase domain (CTD); NTD plays a key role in substrate phosphorylation; Val82 and Lys100 in the NTD are critical for kaempferol binding and RSK2 activity, established by homology modeling, mutagenesis, and small-molecule docking. |
Mutagenesis (Val82, Lys100), homology model + docking validated by mutagenesis, kinase activity assay, domain deletion experiments |
Cancer research |
Medium |
19435896
|
| 2010 |
RSK2 phosphorylates caspase-8 at Thr-263, promoting caspase-8 ubiquitination and proteasomal degradation in response to EGF; RSK2 thereby blocks Fas-induced apoptosis through phosphorylation of caspase-8. |
In vitro kinase assay, site-directed mutagenesis (Thr263), proteasome inhibition assay, Fas-induced apoptosis assay, RSK2 knockout cells |
The Journal of biological chemistry |
Medium |
21183680
|
| 2010 |
ATF1 is a novel substrate of RSK2; RSK2 phosphorylates ATF1 at Ser-63, enhancing ATF1 transcriptional activity; eriodictyol binds the RSK2 NTD (confirmed by crystal structure docking and in vitro pulldown) and inhibits RSK2-mediated ATF1 phosphorylation. |
In vitro kinase assay, crystal structure-based docking, in vitro pulldown, cell-based phosphorylation assay, reporter assay |
The Journal of biological chemistry |
Medium |
21098035
|
| 2011 |
RSK2 directly phosphorylates histone H2AX at both Ser139 and a newly identified site Ser16; EGF-induced phosphorylation at both sites is decreased in RSK2 knockout cells; RSK2-mediated H2AX phosphorylation enhances H2AX stability and prevents EGF-induced cell transformation; RSK2 and DNA-PK (but not ATM/ATR) are required for Ser139 phosphorylation, while only RSK2 is required for Ser16 phosphorylation. |
In vitro kinase assay, RSK2 knockout cells, co-immunoprecipitation, immunofluorescence, cell transformation assay |
Cancer research |
Medium |
21224359
|
| 2012 |
RSK2 mediates Ras/Raf-dependent inactivation of integrins: active RSK2 impairs cell adhesion and fibronectin matrix assembly, promotes cell motility, reduces actin stress fibers, disrupts focal adhesions, co-localizes with the integrin activator talin, promotes filamin phosphorylation and integrin binding, and is itself activated in response to fibronectin ligation. |
RSK2 siRNA knockdown, integrin activation assays, co-localization by immunofluorescence, fibronectin matrix assembly assay, migration assay, co-immunoprecipitation |
The Journal of biological chemistry |
Medium |
23118220
|
| 2013 |
RSK2 phosphorylates PLD1 at Thr-147, activating PLD1 and promoting synthesis of phosphatidic acid at sites of neurite outgrowth; this RSK2→PLD1 pathway controls TiVAMP/VAMP-7 vesicle fusion and is required for NGF-induced neurite outgrowth; phosphomimetic PLD1 rescues neurite outgrowth in RSK2-silenced cells. |
RSK2 and PLD1 knockout mice neurons, siRNA, pharmacological inhibition, TIRF microscopy, phosphomimetic rescue in PC12 cells |
The Journal of neuroscience |
High |
24336713
|
| 2013 |
RSK2-CREB signaling upregulates fascin-1 expression; RSK2 knockdown disrupts filopodia formation and bundling in invasive cancer cells; fascin-1 expression rescues the loss of invasion caused by RSK2 knockdown, establishing the RSK2→CREB→Fascin-1 axis in cancer cell invasion and metastasis. |
siRNA knockdown, RSK2 inhibitor (FMK-MEA), fascin-1 rescue expression, filopodia imaging, invasion assay, in vivo metastasis model |
The Journal of biological chemistry |
Medium |
24085294
|
| 2013 |
RSK2 directly binds and phosphorylates stathmin at Ser16 at the leading edge of cancer cells, reducing stathmin-mediated microtubule depolymerization and promoting microtubule stability; phosphomimetic stathmin-S16D rescues the decreased invasive and metastatic potential caused by RSK2 knockdown. |
Co-immunoprecipitation, in vitro kinase assay, RSK2 siRNA knockdown, phosphomimetic rescue, invasion and metastasis assays |
Oncogene |
Medium |
27041561
|
| 2013 |
RSK2 inhibits apoptosis signal-regulating kinase 1 (ASK1) by phosphorylating Ser83, Thr1109, and Thr1326; phospho-T1109/T1326 inhibits ATP binding to ASK1, and phospho-S83 attenuates ASK1 substrate MKK6 binding; RSK2 also provides antianoikis protection via CREB-mediated upregulation of PTK6 and downregulation of ING3. |
In vitro kinase assay, mutagenesis, ATP-binding assay, substrate binding assay, RSK2 knockdown, anoikis assay, gene expression analysis |
Molecular and cellular biology |
Medium |
23608533
|
| 2013 |
RSK2 phosphorylates TRAF6 at Ser46, Ser47, and Ser48; this phosphorylation is required for TRAF6 K63 ubiquitination, which promotes downstream inflammation signaling (IKKα/β, p38, JNK); RSK2 knockout mice show reduced F4/80 and CD3 infiltration and reduced TRAF6 K63 ubiquitination in colon tissue. |
In vitro kinase assay, RSK2 knockout mice, co-immunoprecipitation, ubiquitination assay, colon inflammation model |
Oncogene |
Medium |
29563609
|
| 2013 |
RSK2 interacts with FGFR1, confirmed by yeast two-hybrid and in vitro/in vivo experiments; phosphorylated RSK2 phosphorylates Ser789 in the C-terminal tail of FGFR1; RSK2 inhibition leads to prolonged FGFR1 tyrosine transphosphorylation; mutation of Ser789 to Ala or RSK2 inhibition reduces FGFR1 endocytosis and ubiquitination, explaining prolonged signaling. |
Yeast two-hybrid, co-immunoprecipitation, in vitro kinase assay, site-directed mutagenesis (S789A), FGFR1 endocytosis assay, ubiquitination assay |
Oncogene |
High |
24141780
|
| 2015 |
RSK2 (but not RSK1) directly interacts with and phosphorylates NHE3 at Ser663 at the apical membrane domain, mediating LPA-induced NHE3 stimulation; Pyk2 maintains PDK1 autophosphorylation required for RSK2 activation upstream of NHE3. |
RSK2-specific siRNA knockdown, co-immunoprecipitation at apical membrane, in vitro phosphorylation assay, Ser663 mutagenesis, NHE3 transport activity assay |
American journal of physiology. Cell physiology |
Medium |
25855080
|
| 2016 |
β-Trcp ubiquitin ligase and RSK2 cooperate to degrade FOXN2; RSK2 phosphorylates FOXN2 at Ser365 and Ser369 in a conserved DSGYAS motif, targeting it for β-Trcp-mediated ubiquitination and proteasomal degradation, which promotes tumor growth and radioresistance in lung cancer. |
Co-immunoprecipitation, in vitro kinase assay, site-directed mutagenesis (Ser365, Ser369), ubiquitination assay, gain/loss-of-function studies |
Cell death and differentiation |
Medium |
29396548
|
| 2017 |
RSK2 directly interacts with leukemia-associated RhoGEF (LARG) and nucleotide-bound Rho isoforms (RhoA, RhoB, RhoC but not Rac1 or Cdc42); EGF/FBS stimulation induces association of endogenous RSK2 with LARG; RSK2 phosphorylates LARG at Ser1288 to activate RhoA; Thr577 phosphorylation on RSK2 is essential for this; RSK2-mediated motility requires RhoA and RhoB but not RhoC. |
Co-immunoprecipitation (endogenous), in vitro kinase assay, mutagenesis (Ser1288, Thr577), RhoA activity assay, migration/invasion assay |
Proceedings of the National Academy of Sciences of the United States of America |
High |
29279389
|
| 2018 |
RSK2 phosphorylates the regulatory myosin light chain (RLC20) at Ser19 in vitro, promoting smooth muscle contractility; RSK2 also phosphorylates an activating site on NHE-1, causing cytosolic alkalinization and increased intracellular Ca2+ that promotes vasoconstriction; Rsk2-deficient mice show dilated resistance arteries, reduced myogenic tone, reduced RLC20 phosphorylation, suppressed NHE-1 activity, and lower blood pressure. |
In vitro kinase assay (RSK2 + RLC20), Rsk2 knockout mice (myogenic tone, blood pressure, pH and Ca2+ measurements), in situ phosphorylation analysis |
Science signaling |
High |
30377223
|
| 2018 |
ERα physically interacts with RSK2 through its N-terminus and sequesters active RSK2 into the nucleus, where it activates a proneoplastic transcriptional network; antiestrogens disrupt the RSK2–ERα interaction, driving RSK2 into the cytoplasm; transgenic mice with stable nuclear RSK2 in the mammary gland develop high-grade ductal carcinoma in situ. |
Co-immunoprecipitation, nuclear fractionation, transgenic mouse model, in vitro and in vivo breast cancer models |
Cancer research |
Medium |
29351904
|
| 2019 |
RSK2 directly interacts with ELK3 through its N-terminal kinase and linker domains binding to the D and C domains of ELK3, phosphorylates ELK3, and enhances c-fos promoter activity via ELK3; RSK2 deficiency reduces ELK3 nuclear localization. |
Co-immunoprecipitation (domain mapping), kinase assay, reporter assay (c-fos promoter), immunocytofluorescence, RSK2 knockdown/knockout |
International journal of molecular sciences |
Medium |
31018569
|
| 2020 |
RSK2-inactivating mutations in HCC attenuate a SOS1/2-dependent negative feedback loop, leading to activation of MAPK signaling; restoring RSK2 expression in RSK2-null HCC cells suppresses proliferation and migration in vitro and tumorigenicity in vivo. |
Exome sequencing, RSK2 re-expression in natural RSK2-null cells, RNA-seq, qRT-PCR, mass spectrometry, xenograft tumor model |
Journal of hepatology |
Medium |
32918955
|
| 2020 |
RSK2 directly binds AMPKα2 in the nucleus and phosphorylates it at Thr172, promoting autophagy under ER stress; IRE1α (ER membrane UPR sensor) is required for ERK1/2-RSK2 activation under ER stress; suppression of RSK2-mediated autophagy enhances sensitivity to ER stress-inducing agents. |
Co-immunoprecipitation, in vitro kinase assay (RSK2 + AMPKα2), IRE1α knockdown, RSK2 knockdown, autophagy assay, in vivo xenograft |
Oncogene |
Medium |
32958832
|
| 2020 |
TGF-β activates ERK and RSK2, causing nuclear translocation of phosphorylated RSK2, which then phosphorylates VGLL1 at Ser84; phosphorylated VGLL1 acts as a transcription cofactor of TEAD4, activating MMP9 transcription to promote gastric cancer malignancy. |
Site-directed mutagenesis (Ser84), co-immunoprecipitation, EMSA, ChIP assay, immunoprecipitation, reporter assay |
Biochimica et biophysica acta. Molecular cell research |
Medium |
33069758
|
| 2022 |
GDH1 (phosphorylated by EGFR at Tyr135) and RSK2 cooperate to enhance CREB activity via CaMKIV signaling, promoting lung cancer metastasis; co-targeting RSK2 and GDH1 synergistically attenuates cancer cell invasion, anoikis resistance, and immune escape. |
siRNA knockdown, pharmacological inhibition, kinase assay, invasion/anoikis assay, CD8 T cell infiltration analysis, patient tumor correlation |
Cell reports |
Medium |
36516759
|
| 2023 |
RSK2 controls RPS6 phosphorylation in neurons, which is essential for peripheral and central nervous system axon regeneration; RSK2 controls the peripheral nerve preconditioning effect; the RSK2-RPS6 axis drives CNS regeneration in the dorsal column, synaptic plasticity, and target innervation leading to functional recovery. |
RSK2 knockout mice, in vivo axon injury/regeneration assay, DRG neuron culture, adeno-associated virus shRNA knockdown, electrophysiology |
PLoS biology |
Medium |
37068088
|
| 2012 |
RSK2 functions in the medial habenula to contribute to acute morphine analgesia; RSK2 knockout reduces acute morphine analgesia in the tail immersion test; AAV-mediated RSK2 knockdown specifically in the habenula recapitulates the reduced analgesia, suggesting a mu opioid receptor-RSK2 signaling mechanism in this brain region. |
RSK2 knockout mice, AAV-mediated shRNA knockdown in habenula, tail immersion test |
Neuropsychopharmacology |
Medium |
22218090
|
| 2009 |
RSK2 knockdown in cells enhances influenza virus polymerase activity and viral growth; RSK2 knockdown reduces NF-κB- and IFN-β-dependent promoter stimulation in response to influenza; RSK2 knockdown suppresses influenza-induced PKR phosphorylation, placing RSK2 upstream of PKR in the innate antiviral response. |
siRNA knockdown, viral polymerase activity assay, reporter assays (NF-κB, IFN-β), PKR phosphorylation assay |
Journal of virology |
Medium |
19129453
|
| 2003 |
RSK2-deficient cells are defective for UV-induced STAT3 Ser727 phosphorylation, restored by ectopic RSK2 re-expression; active RSK2 induces phosphorylation of STAT3 immunoprecipitates in vitro, requiring a cofactor or downstream kinase; ATM is required upstream for UVA-stimulated RSK2 activation. |
RSK2-deficient cells, rescue by ectopic RSK2 expression, in vitro kinase assay on STAT3 immunoprecipitates, dominant-negative STAT3-β, reporter assay |
The Journal of biological chemistry |
Low |
12562765
|
| 2010 |
RSK2 interacts with and phosphorylates GSK3β at Ser9, inhibiting GSK3β activity; RSK2-deficient MEFs show reduced GSK3β Ser9 phosphorylation upon EGF and calcium ionophore stimulation. |
Co-immunoprecipitation, in vitro kinase assay, RSK2 knockout MEFs, rescue by RSK2 re-expression |
Biochemical and biophysical research communications |
Low |
24055036
|
| 2014 |
RSK2 deficiency in TNF-α transgenic mice results in earlier and exacerbated arthritis with increased inflammatory cytokine production, MMP activity, and osteoclastogenic molecules; bone marrow from RSK2-null mice fails to transfer this phenotype, indicating RSK2 expression in mesenchymal (synovial fibroblast) cells controls synoviocyte hyperplasia and the course of arthritis. |
RSK2 knockout in TNFtg arthritis model, bone marrow transplant, in vitro FLS characterization, gene expression profiling |
Annals of the rheumatic diseases |
Medium |
25414238
|
| 2010 |
RSK2 knockdown in cortical radial precursors (by shRNA in vitro and in utero electroporation in vivo) decreases neurogenesis and increases the proportion of proliferating Pax6-positive radial precursor cells, establishing that RSK2 is required for cortical radial precursors to differentiate into neurons (but is not required for astrocyte generation). |
shRNA knockdown in primary cortical precursors, in utero electroporation, immunostaining for neuronal and progenitor markers |
Developmental biology |
Medium |
20832397
|