YWHAE Antibody

What is YWHAE and why is it important in cellular research?

YWHAE (14-3-3 protein epsilon) is an adapter protein that regulates numerous general and specialized signaling pathways. Its importance stems from its ability to bind multiple partners through recognition of phosphoserine or phosphothreonine motifs, thereby modulating their activity . YWHAE plays crucial roles in:

• Regulating phosphorylated HSF1 nuclear export to the cytoplasm

• Facilitating antiviral signaling pathways upstream of TBK1 via RIGI interaction

• Controlling RIGI redistribution from cytosol to mitochondrial membranes during viral infections

• Inhibiting cell proliferation and promoting cell cycle arrest through nuclear-cytoplasmic transport of proteins like HNRNPC

These diverse functions make YWHAE a valuable research target for understanding fundamental cellular processes and disease mechanisms.

What are the known isoforms of YWHA family proteins and how do they differ from YWHAE?

The YWHA (14-3-3) protein family consists of seven mammalian isoforms that have been identified in various tissues including mouse oocytes and eggs:

While all isoforms share structural similarities, they have distinct tissue distributions and binding partners. YWHAE specifically has been shown to have essential roles in embryonic development, as global knockout mice die at birth due to cardiac malformations .

What experimental methods are suitable for detecting YWHAE expression in tissue samples?

Multiple complementary approaches can be used to detect YWHAE expression in tissue samples:

• Immunoblotting (Western blot): Using isoform-specific antibodies like rabbit monoclonal antibodies that recognize human, rat, and mouse YWHAE . This approach provides quantitative information about protein expression levels.

• RT-PCR: Used to detect YWHAE mRNA in tissues. Isoform-specific primers can amplify YWHAE transcripts, which can be confirmed by sequencing the PCR products .

• RNA sequencing: Single-cell RNA-seq can identify YWHAE transcripts and provide FPKM (fragments per kilobase of exon model per million reads mapped) values to estimate expression levels .

• Immunofluorescence microscopy: Using isoform-specific antibodies to visualize the cellular distribution of YWHAE protein in tissue sections or cultured cells .

• Proximity Ligation Assay (PLA): A sensitive method to detect protein-protein interactions involving YWHAE at the molecular level with high specificity .

When designing experiments, it's important to use appropriate controls and validate antibody specificity, as cross-reactivity between 14-3-3 isoforms can occur.

How can I validate the specificity of YWHAE antibodies for my experiment?

Validating antibody specificity is critical for obtaining reliable results. For YWHAE antibodies, consider these methodological approaches:

• Positive and negative control samples: Use tissues or cell lines known to express or lack YWHAE. For negative controls, YWHAE knockout cells/tissues are ideal .

• Blocking peptide competition: Pre-incubate the antibody with the immunizing peptide before application to verify signal reduction.

• Knockdown verification: Compare antibody reactivity in wild-type versus YWHAE knockdown or knockout samples. Research has generated YWHAE knockout mice that can provide definitive negative controls .

• Cross-reactivity testing: Test the antibody against recombinant proteins of all seven 14-3-3 isoforms to ensure it specifically recognizes YWHAE.

• Multiple antibody comparison: Use different antibodies targeting different epitopes of YWHAE to confirm consistent results.

• Immunoprecipitation followed by mass spectrometry: This can confirm that the antibody is pulling down YWHAE rather than other 14-3-3 family members.

The research literature demonstrates successful use of isoform-specific antibodies to distinguish all seven mammalian YWHA proteins in mouse oocytes and eggs .

What are the optimal protocols for studying YWHAE protein-protein interactions in different cell types?

Studying YWHAE interactions requires techniques that preserve physiological binding while providing specificity. Based on research findings, these methodological approaches are most effective:

• Proximity Ligation Assay (PLA): This highly sensitive technique has been successfully used to detect interactions between YWHAE and CDC25B at the single molecule level directly in cells . The method:

  • Requires primary antibodies against YWHAE and its potential binding partner

  • Provides visualization of actual intracellular interaction sites

  • Offers high signal-to-noise ratio due to signal amplification

  • Requires proteins to be within 40 nm of each other

  • Allows visualization of interaction sites as distinct fluorescent spots

• Förster Resonance Energy Transfer (FRET): Used to demonstrate interactions between YWHAH (a related isoform) and CDC25B, this technique can be adapted for YWHAE studies . FRET requires:

  • Fluorescent protein tagging (e.g., mCherry-YWHAE, EGFP-partner protein)

  • Live-cell imaging capability

  • Analysis of energy transfer between fluorophores

• Co-immunoprecipitation with isoform-specific antibodies: When performing co-IP with YWHAE antibodies:

  • Use gentle lysis buffers to preserve interactions

  • Include phosphatase inhibitors to maintain phosphorylation-dependent interactions

  • Validate with reciprocal IP experiments

  • Consider crosslinking for transient interactions

• Expression of fluorescently tagged YWHAE: mRNA constructs expressing fluorescently labeled proteins (e.g., mCherry-YWHAH and EGFP-YWHAE) have been successfully used to study the distribution of these proteins in mouse oocytes .

When interpreting results, it's important to note that differences in primary antibody binding affinities can affect quantitative comparisons between different YWHA isoform interactions .

How do YWHAE knockout or knockdown models compare with pharmacological inhibition for studying YWHAE function?

Different approaches to inhibiting YWHAE function have distinct advantages and limitations for research applications:

Research findings indicate that oocyte-specific or global elimination of YWHAE does not alter oocyte maturation, in vitro fertilization, or early development, though global inactivation impairs in vivo fertility . This suggests that functional redundancy among YWHA isoforms may compensate for the loss of individual members.

What methodological approaches are recommended for studying YWHAE in skin disorders such as atopic dermatitis?

Research has implicated YWHAE in skin conditions, particularly atopic dermatitis (AD) and tyrosinase-mediated pigmentation . Recommended methodological approaches include:

• YWHAE overexpression in keratinocytes: HaCaT human keratinocytes have been successfully used as a model system for YWHAE overexpression studies .

• High-throughput screening (HTS) approaches:

  • RNA sequencing to identify differentially expressed genes

  • Antibody arrays to identify protein-level changes

  • Integrated bioinformatics analysis

• Validation of YWHAE-associated factors: Several novel genes associated with YWHAE function in keratinocytes have been identified and should be considered in experimental design:

  • Keratin-related genes: KRT9, KRT1, KRT6C

  • Signaling molecules: MAPK1, MAPK15, TYK2, NOS3

  • Cellular structure proteins: TUBA1A, ACTC1

  • Immune-related genes: BST2, IFI27, MX2

  • Cell death regulators: CASP3

• Protein-protein interaction analysis: CD37 was validated as a unique gene detected across multiple methodologies, suggesting its importance in YWHAE function in skin .

• Functional assays: Based on the KEGG pathway analysis, examining YWHAE's effects on:

  • Cell cycle regulation

  • Apoptosis pathways

  • Inflammatory signaling

  • Matrix metalloproteinase activity (MMP2)

These approaches provide complementary information about YWHAE's role in skin biology and pathology, which is essential for understanding its contribution to atopic dermatitis.

How can researchers differentiate between the roles of different YWHA isoforms when they appear to have redundant functions?

Differentiating between redundant YWHA isoforms presents a significant challenge. Based on research findings, these methodological approaches have proven effective:

• Double or multiple knockout models: Creating double knockouts (e.g., YWHAH and YWHAE) has been used to address potential compensatory mechanisms between isoforms . This approach can reveal phenotypes not apparent in single knockouts.

• Isoform-specific antibodies for interaction studies: Using carefully validated isoform-specific antibodies in proximity ligation assays (PLA) can identify specific interactions between individual YWHA isoforms and binding partners like CDC25B .

• Quantitative expression analysis across tissues: RNA-seq data from various tissues and developmental stages can identify differential expression patterns of YWHA isoforms, providing clues about tissue-specific functions .

• Isoform-specific morpholino oligonucleotides: Translation-blocking morpholinos targeting specific isoforms have been used to explore their individual roles .

• Expression of dominant-negative mutants: These can selectively interfere with specific isoform functions while leaving others intact.

• CRISPR-Cas9 genome editing: Creating cell lines with specific isoform modifications can provide clean systems for studying individual YWHA proteins.

Research findings suggest that while single isoform deletion (either YWHAH or YWHAE) does not prevent oocyte maturation or early development, isoform-specific effects may be more apparent in other tissues or physiological contexts .

What are the critical considerations when using YWHAE antibodies for studying protein localization during cell cycle progression?

When investigating YWHAE localization during cell cycle events, several methodological considerations are important:

• Fixation and permeabilization protocols: YWHAE's distribution between cytoplasm and nucleus can vary during cell cycle progression. Studies have shown that YWHAE is primarily cytoplasmic in mouse oocytes, with less nuclear localization . Consider:

  • Comparing different fixation methods (paraformaldehyde vs. methanol)

  • Testing different permeabilization protocols to ensure antibody access

  • Preserving phosphorylation status that may affect YWHAE interactions

• Cell cycle synchronization methods:

  • For oocytes: Use of dbcAMP or IBMX to maintain meiotic arrest

  • For somatic cells: Thymidine block, nocodazole treatment, or serum starvation

  • Consider that synchronization methods themselves may affect YWHAE phosphorylation or localization

• Live-cell imaging approaches: Expression of fluorescently tagged YWHAE proteins (e.g., mCherry-YWHAE) allows real-time tracking of localization changes . Consider:

  • Using minimal expression levels to avoid artifacts

  • Validating that tagged proteins behave like endogenous YWHAE

  • Co-expressing cell cycle markers

• Co-localization with cell cycle regulators: YWHAE interacts with CDC25B and may sequester it in the cytoplasm of prophase I-arrested oocytes . Examining co-localization with:

  • CDC25B and other cell cycle phosphatases

  • Cyclins and CDKs

  • Nuclear envelope components

• Phosphorylation-specific antibodies: Since YWHAE binding often depends on phosphorylation of target proteins, phospho-specific antibodies may provide insight into functional interactions during cell cycle progression.

Research has demonstrated that fluorescently labeled YWHAE proteins efficiently express in mouse oocytes, with primarily cytoplasmic distribution and less nuclear localization, providing a foundation for cell cycle localization studies .

How can YWHAE antibodies be employed to investigate its role in antiviral signaling pathways?

Recent research has revealed YWHAE's involvement in antiviral signaling, presenting new opportunities for investigation using YWHAE antibodies:

• Proximity ligation assays (PLA) for interaction mapping: YWHAE plays a positive role in the antiviral signaling pathway upstream of TBK1 via interaction with RIGI . PLA techniques that have successfully demonstrated YWHAE-CDC25B interactions can be adapted to study:

  • YWHAE-RIGI interactions in different cell types

  • Dynamic changes in these interactions during viral infection

  • Effects of interferon stimulation on interaction patterns

• Subcellular fractionation with immunoblotting: Since YWHAE directs RIGI redistribution from the cytosol to mitochondrial associated membranes during viral infection , researchers should:

  • Isolate mitochondrial, cytosolic, and membrane fractions

  • Probe fractions with YWHAE antibodies before and after viral stimulation

  • Co-immunoprecipitate YWHAE from different fractions to identify compartment-specific binding partners

• Live-cell imaging with fluorescent-tagged proteins: Building on techniques used to study YWHAE distribution in oocytes :

  • Track YWHAE-RIGI colocalization during viral infection

  • Measure kinetics of redistribution to mitochondrial membranes

  • Correlate localization changes with activation of downstream signaling

• YWHAE knockdown/knockout effect on MAVS activation: Since YWHAE mediates MAVS-dependent innate immune signaling :

  • Use YWHAE antibodies to compare MAVS oligomerization states in control vs. YWHAE-deficient cells

  • Examine phosphorylation status of TBK1 and IRF3 in response to viral infection

  • Measure interferon production as a functional readout

These approaches will help elucidate the mechanisms by which YWHAE contributes to antiviral immunity, potentially revealing new therapeutic targets for viral infections.

What are the methodological challenges when using YWHAE antibodies to study its interactions with CDC25B in different cell types?

Research has established that YWHAE interacts with CDC25B in mouse oocytes , but studying these interactions across different cell types presents several methodological challenges:

• Tissue-specific expression levels: YWHAE and CDC25B expression varies across tissues, requiring:

  • Preliminary quantification of expression levels in target tissues

  • Optimization of antibody concentrations for each tissue type

  • Careful selection of positive and negative control tissues

• Phosphorylation-dependent interactions: Since YWHAE binds to phosphorylated motifs , researchers must:

  • Preserve phosphorylation status during sample preparation

  • Use phosphatase inhibitors in all buffers

  • Consider immunoprecipitation with phospho-specific antibodies

  • Compare interactions under different kinase/phosphatase activity conditions

• Technical limitations of proximity ligation assay (PLA):

  • PLA results can be affected by primary antibody binding affinities

  • Quantitative comparisons between different YWHA isoforms may be challenging

  • Only a portion of protein-protein interactions are detected

  • Optimization required for each cell type (fixation, antibody concentration, amplification time)

• Distinguishing direct vs. indirect interactions: Determine whether YWHAE-CDC25B binding is direct or mediated by other proteins through:

  • In vitro binding assays with purified proteins

  • Crosslinking prior to immunoprecipitation

  • Mass spectrometry analysis of interaction complexes

• Cell cycle-dependent variation: Since CDC25B activity is cell cycle-regulated, interactions may vary temporally, requiring:

  • Synchronization methods appropriate for each cell type

  • Time-course analyses following release from synchronization

  • Single-cell analyses to account for asynchrony

Addressing these challenges requires careful experimental design and validation using multiple complementary approaches, as demonstrated in successful studies of YWHAE-CDC25B interactions in oocytes .

How can multi-omics approaches enhance our understanding of YWHAE function when integrated with antibody-based techniques?

Multi-omics integration with antibody-based detection offers powerful insights into YWHAE function. Research has successfully employed this approach in keratinocytes , providing a methodological framework:

• RNA sequencing integrated with antibody arrays: This combination has identified novel YWHAE-associated genes in keratinocytes . Implementation requires:

  • YWHAE overexpression or knockdown in target cells

  • Parallel RNA-seq and protein antibody array analysis

  • Bioinformatic integration of transcriptomic and proteomic datasets

  • Validation of key targets using YWHAE antibodies

• Bioinformatics algorithms for pathway analysis: Apply computational tools to:

  • Identify enriched biological pathways (KEGG, Gene Ontology)

  • Construct protein-protein interaction networks

  • Predict functional outcomes of YWHAE modulation

  • Prioritize targets for validation

• Validation strategies for multi-omics findings:

  • Confirm RNA expression changes with RT-qPCR

  • Validate protein changes with YWHAE antibodies in Western blots

  • Verify protein-protein interactions with co-immunoprecipitation

  • Assess functional outcomes with appropriate cell-based assays

• Single-cell approaches for heterogeneous populations:

  • Single-cell RNA-seq to identify cell-specific YWHAE functions

  • Mass cytometry with YWHAE antibodies to correlate with other markers

  • Spatial transcriptomics to map YWHAE activity in complex tissues

Research using this integrated approach has identified several novel YWHAE-associated genes including KRT9, KRT1, KRT6C, BST2, CIB2, APH1B, ACTC1, IFI27, TUBA1A, CAPN6, UTY, MX2, MAPK15, MAPK1, MMP2, TYK2, NOS3, and CASP3, with CD37 being uniquely validated across all methodologies .

What is the significance of YWHAE in neural development and how can antibody-based approaches be optimized for studying its function in neural tissues?

While the search results don't directly address YWHAE's role in neural development, they mention that global YWHAE knockout mice show hippocampal and cortical defects , suggesting important neural functions. Optimizing antibody-based approaches for neural tissues requires:

• Developmental timing considerations:

  • Examine YWHAE expression across neural development stages using timed collections

  • Compare embryonic, postnatal, and adult YWHAE distribution in neural tissues

  • Correlate expression patterns with neurogenesis, migration, and differentiation markers

• Neural cell type-specific analysis:

  • Use YWHAE antibodies in combination with neural cell type markers

  • Implement fluorescence-activated cell sorting (FACS) with YWHAE antibodies

  • Perform immunohistochemistry on brain sections to map regional distribution

• Specialized tissue preparation techniques:

  • Optimize fixation protocols for neural tissues (perfusion vs. immersion)

  • Test antigen retrieval methods for improved YWHAE detection

  • Consider specialized permeabilization for synaptic compartments

• Functional assays in neural contexts:

  • Examine effects of YWHAE knockdown on neuronal morphology and connectivity

  • Assess impact on electrophysiological properties

  • Investigate axonal transport and synaptic function

• Protein-protein interactions in neural context:

  • Identify neural-specific YWHAE binding partners through co-immunoprecipitation

  • Apply proximity ligation assay (PLA) to brain sections or cultured neurons

  • Investigate interactions with neural-specific signaling molecules

Given that YWHAZ (another 14-3-3 family member) knockout mice show neurological defects , comparative studies between different 14-3-3 isoforms in neural tissues could provide valuable insights into their specialized or redundant functions in the nervous system.

What are the best practices for optimizing Western blot protocols when using YWHAE antibodies?

When using YWHAE antibodies for Western blotting, these technical considerations improve results:

• Sample preparation optimization:

  • Include phosphatase inhibitors to preserve phosphorylation-dependent interactions

  • Use gentle lysis buffers (e.g., RIPA or NP-40 based) to maintain protein structure

  • Determine optimal protein loading (typically 20-40 μg total protein)

  • Consider subcellular fractionation to enrich for YWHAE in relevant compartments

• Electrophoresis and transfer parameters:

  • YWHAE molecular weight is approximately 29 kDa - optimize gel percentage accordingly (12-15%)

  • Use gradient gels for examining both YWHAE and its higher molecular weight binding partners

  • Optimize transfer conditions (wet transfer often provides better results for YWHAE)

  • Consider PVDF membranes for higher protein binding capacity

• Antibody selection and validation:

  • Commercial rabbit monoclonal YWHAE antibodies have been validated for Western blot applications with human, rat, and mouse samples

  • Determine optimal primary antibody dilution (typically 1:1000 - 1:5000)

  • Include proper positive controls (recombinant YWHAE or lysates from cells expressing YWHAE)

  • Include negative controls (YWHAE knockout tissues where available)

• Signal detection and quantification:

  • Compare chemiluminescence vs. fluorescent detection methods

  • For quantitative analysis, ensure signal is within linear range

  • Use housekeeping proteins appropriate for your experimental context

  • Consider stripping and reprobing membranes to examine YWHAE binding partners

• Troubleshooting common issues:

  • For high background: Increase blocking time/concentration or try different blocking agents

  • For weak signal: Increase antibody concentration, protein loading, or exposure time

  • For multiple bands: Verify specificity with knockout controls or alternative antibodies

Following these practices will help ensure specific and sensitive detection of YWHAE protein in Western blot applications.

How can researchers effectively use YWHAE antibodies in immunoprecipitation experiments to identify novel binding partners?

Immunoprecipitation (IP) with YWHAE antibodies is a powerful approach for discovering novel interactions. Based on research methodologies, consider these optimizations:

• Antibody selection for immunoprecipitation:

  • Test multiple YWHAE antibodies recognizing different epitopes

  • Consider using tag-based approaches (e.g., expressing tagged YWHAE) as an alternative

  • Validate IP efficiency by Western blotting a small portion of the immunoprecipitate

  • Determine optimal antibody-to-lysate ratios

• Lysis and IP buffer optimization:

  • Since YWHAE binds phosphorylated motifs , always include phosphatase inhibitors

  • Test different detergent conditions (NP-40, CHAPS, Triton X-100) to preserve interactions

  • Include protease inhibitors to prevent degradation

  • Consider salt concentration effects on interaction stability

• Cross-linking strategies:

  • For transient interactions, consider membrane-permeable crosslinkers before lysis

  • DSP (dithiobis[succinimidyl propionate]) allows reversal of crosslinking with reducing agents

  • Formaldehyde can be used for in vivo crosslinking

  • Optimize crosslinker concentration and incubation time

• Mass spectrometry sample preparation:

  • Include appropriate controls (IgG, YWHAE knockout cells)

  • Consider SILAC or TMT labeling for quantitative comparison

  • Perform on-bead digestion to minimize contamination

  • Include multiple biological replicates

• Bioinformatic analysis of identified proteins:

  • Filter against common contaminant databases

  • Look for enrichment of phosphorylated proteins

  • Perform motif analysis for YWHAE binding consensus sequences

  • Validate top candidates with reverse co-IP experiments

Research has shown that YWHAE interacts with multiple partners, including CDC25B in oocytes , and plays roles in processes ranging from antiviral signaling to cell cycle regulation , suggesting many potential novel interactions remain to be discovered.

What controls and validation steps are essential when using YWHAE antibodies in immunohistochemistry or immunofluorescence?

When performing immunohistochemistry (IHC) or immunofluorescence (IF) with YWHAE antibodies, these controls and validation steps are critical:

• Positive and negative tissue controls:

  • Positive controls: Tissues known to express YWHAE (widely expressed in multiple tissues)

  • Negative controls: YWHAE knockout tissues where available

  • Developmental controls: Tissues at stages before YWHAE expression begins

• Antibody validation controls:

  • Primary antibody omission: Reveals non-specific secondary antibody binding

  • Isotype control: Non-specific primary antibody of same isotype and concentration

  • Absorption control: Pre-incubation of antibody with immunizing peptide

  • Comparative antibody approach: Testing multiple antibodies against different YWHAE epitopes

• Fixation and antigen retrieval optimization:

  • Compare aldehyde vs. alcohol-based fixatives

  • Test multiple antigen retrieval methods (heat-induced vs. enzymatic)

  • Optimize fixation duration for your specific tissue

  • Validate that fixation preserves protein localization

• Signal specificity verification:

  • Verify subcellular localization matches known YWHAE distribution (primarily cytoplasmic with less nuclear localization in oocytes)

  • Compare IF results with subcellular fractionation followed by Western blotting

  • Use siRNA or morpholino knockdown to confirm signal reduction

  • Consider fluorescently tagged YWHAE expression to compare with antibody staining

• Multiplexing considerations:

  • When co-staining with other antibodies, verify lack of cross-reactivity

  • Ensure secondary antibodies don't cross-react

  • Include appropriate single-stain controls

  • Verify spectral separation when using multiple fluorophores

Research has successfully used fluorescently labeled YWHAE to study its distribution in mouse oocytes, showing primarily cytoplasmic localization with less nuclear distribution , providing a reference point for validating antibody-based localization studies.

What are the most promising future directions for YWHAE antibody research?

Based on current findings, several promising research directions emerge for YWHAE antibody applications:

• Therapeutic targeting of YWHAE interactions: Given YWHAE's role in atopic dermatitis and various signaling pathways , developing antibodies or small molecules that modulate specific YWHAE interactions could have therapeutic potential.

• Single-cell analysis of YWHAE function: Advancing techniques to study YWHAE at the single-cell level will reveal cell-type specific functions and heterogeneity in regulatory networks.

• Structural studies of YWHAE-partner complexes: Developing antibodies that recognize specific YWHAE-partner interfaces could provide insights into the structural basis of these interactions.

• Isoform-specific functions in development and disease: Further exploration of the unique and redundant functions of YWHAE compared to other 14-3-3 family members will enhance our understanding of their biological roles.

• YWHAE in antiviral immunity: Expanding research on YWHAE's role in antiviral signaling could reveal new mechanisms of host defense and potential therapeutic targets.

• Tissue-specific knockout models: Developing additional tissue-specific YWHAE knockout models beyond oocyte-specific knockouts will help define its role in different physiological contexts.

• YWHAE in neurodevelopmental processes: Given the hippocampal and cortical defects observed in YWHAE knockout mice , further investigation of its neural functions is warranted.

These directions will benefit from continued refinement of antibody-based techniques and their integration with emerging technologies in proteomics, genomics, and imaging.

How can researchers integrate YWHAE antibody-based findings with other experimental approaches to gain comprehensive insights?

A multilayered experimental strategy provides the most comprehensive understanding of YWHAE function:

• Complementary genomic and proteomic approaches: Integrate YWHAE antibody-based findings with:

  • CRISPR-Cas9 genetic screens to identify functional pathways

  • RNA-seq and antibody arrays as successfully implemented in keratinocyte studies

  • Phosphoproteomic analysis to identify YWHAE-dependent phosphorylation changes

  • ChIP-seq to identify transcriptional changes downstream of YWHAE signaling

• Multi-scale analysis from molecules to organisms:

  • In vitro biochemical studies of purified YWHAE interactions

  • Cellular assays using YWHAE antibodies for localization and interaction studies

  • Tissue-specific analyses in normal and disease states

  • Whole-organism phenotyping of conditional knockout models

• Temporal dynamics investigation:

  • Real-time imaging with fluorescently tagged YWHAE

  • Time-course studies following stimulation or developmental progression

  • Cell cycle-synchronized analyses

  • Developmental stage-specific examinations

• Computational modeling and prediction:

  • Network analysis of YWHAE interactome data

  • Molecular dynamics simulations of YWHAE-partner interactions

  • Machine learning approaches to predict context-specific functions

  • Integration of multi-omics datasets to build predictive models

• Translational research connections:

  • Connect basic YWHAE biology to disease mechanisms

  • Develop biomarkers based on YWHAE interactions or modifications

  • Screen for therapeutic compounds that modulate specific YWHAE functions

  • Assess YWHAE status in patient samples from relevant conditions