FNBP1L Antibody

What is FNBP1L and why is it important in cellular research?

FNBP1L (Formin Binding Protein 1-Like) is a 605-amino acid protein encoded by the FNBP1L gene in humans that coordinates membrane tubulation with actin cytoskeleton reorganization during endocytosis. It contains a C-terminal Src homology 3 domain (SH3) and an N-terminal extended FER-CIP4 homology domain (EFC) that can bind and deform plasma membranes . The protein localizes to the cell membrane, cytoplasmic vesicles, and cytoplasm, and is widely expressed across multiple tissue types . FNBP1L's importance stems from its involvement in fundamental cellular processes including endocytosis, cell motility, and more recently discovered roles in cancer cell survival pathways such as FAK/PI3K/AKT signaling . Additionally, research has identified FNBP1L as a factor that limits HIV-1 infection in dendritic cells, suggesting its potential role in innate immunity against viral pathogens .

How do I select the appropriate FNBP1L antibody for my specific research needs?

When selecting an FNBP1L antibody, consider these research-specific criteria:

• Epitope recognition: Determine whether you need an N-terminal or C-terminal targeting antibody based on your research questions. For instance, if you're studying protein-protein interactions involving the SH3 domain, a C-terminal antibody may be more appropriate .

• Application compatibility: Verify validated applications for each antibody candidate. From the available data, FNBP1L antibodies have been validated for:

  • Western Blotting (WB)

  • Immunohistochemistry (IHC-P)

  • Immunofluorescence (IF/ICC)

  • ELISA

• Species reactivity: Ensure compatibility with your experimental model. Most commercial antibodies react with human, mouse, and rat FNBP1L .

• Clonality considerations: Polyclonal antibodies offer broader epitope recognition but with potential batch variability, while monoclonal antibodies provide consistent specificity to a single epitope .

• Validation evidence: Review scientific data images showing antibody performance in applications similar to yours, such as the Western blot data showing FNBP1L detection in mouse brain tissue lysate .

What are the key differences between FNBP1L and related proteins like FNBP1?

FNBP1L (also known as TOCA1) and FNBP1 (also called FBP17) are related F-BAR domain-containing proteins with both overlapping and distinct functions:

While both proteins share structural similarities and participate in membrane remodeling, recent research indicates FNBP1 plays a crucial role in maintaining the activity of focal adhesion kinase (FAK) by promoting cell adhesion in cervical cancer cells . In contrast, FNBP1L has been identified as a factor that restricts HIV-1 infection in dendritic cells, suggesting specialized roles in host defense mechanisms .

What are the optimal protocols for using FNBP1L antibodies in Western blot applications?

For optimal Western blot results with FNBP1L antibodies, follow this methodological approach:

Sample Preparation:

• Extract protein from tissues/cells using a lysis buffer containing protease inhibitors

• Quantify protein concentration (Bradford or BCA assay)

• Prepare 20-50 μg of total protein per lane

• Denature samples at 95°C for 5 minutes in loading buffer containing SDS and β-mercaptoethanol

SDS-PAGE and Transfer:

• Separate proteins on 8-10% polyacrylamide gels (FNBP1L is approximately 65-70 kDa)

• Transfer to PVDF or nitrocellulose membrane at 100V for 60-90 minutes

Antibody Incubation:

• Block membrane with 5% non-fat milk or BSA in TBST for 1 hour at room temperature

• Incubate with primary FNBP1L antibody at 1 μg/ml dilution in blocking buffer overnight at 4°C

• Wash 3x with TBST (10 minutes each)

• Incubate with appropriate HRP-conjugated secondary antibody at 1:5000 dilution for 1 hour

• Wash 3x with TBST (10 minutes each)

• Develop using chemiluminescent substrate

Validation Controls:

• Include a positive control (mouse brain tissue lysate has been validated)

• Run a peptide competition assay by pre-incubating antibody with blocking peptide to confirm specificity

• Include molecular weight markers to confirm target band size

The Western blot should show a specific band at approximately 65-70 kDa corresponding to FNBP1L. Validation data has shown successful detection of FNBP1L in mouse brain tissue lysate, with reduced signal in the presence of blocking peptide, demonstrating antibody specificity .

How should I optimize immunohistochemistry protocols for FNBP1L detection in different tissue types?

Optimizing immunohistochemistry (IHC) protocols for FNBP1L detection requires tissue-specific considerations:

General Protocol Framework:

• Fixation: Use 10% neutral buffered formalin fixation (4-24 hours depending on tissue thickness)

• Antigen Retrieval: Heat-induced epitope retrieval (HIER) in citrate buffer (pH 6.0) for 20 minutes

• Blocking: 5-10% normal serum matching the secondary antibody host species, plus 1% BSA in PBS

• Primary Antibody: Apply FNBP1L antibody at 2.5 μg/ml concentration

• Detection System: Use biotin-streptavidin or polymer-based detection systems

• Counterstaining: Hematoxylin for nuclear visualization

Tissue-Specific Optimization Strategies:

Critical Validation Elements:

• Always include positive control tissue (human brain tissue has been validated)

• Include negative controls by omitting primary antibody

• Run peptide competition controls by pre-incubating antibody with blocking peptide

• Validate findings with dual approach (e.g., complement IHC with immunofluorescence)

For neuronal tissues, successful staining has been demonstrated with FNBP1L antibodies at 2.5 μg/ml concentration, visualizing expression patterns in human brain tissues . When examining tissues with potential low expression, consider signal amplification methods such as tyramide signal amplification or extending chromogen development time.

What approaches can be used to confirm FNBP1L antibody specificity in experimental systems?

Confirming FNBP1L antibody specificity is critical for generating reliable research results. Multiple complementary approaches should be employed:

Peptide Competition Assay:

• Pre-incubate the FNBP1L antibody with excess immunizing peptide (5-10× molar excess)

• Apply both blocked and unblocked antibody to duplicate samples

• Compare signal reduction in the blocked condition

• Successful validation should show significantly reduced or eliminated signal

Genetic Knockdown/Knockout Validation:

• Generate FNBP1L knockdown cells using RNA interference or CRISPR-Cas9 technology

• Compare antibody staining between control and knockdown samples

• Quantify reduction in signal intensity proportional to knockdown efficiency

• This approach has been utilized to confirm antibody specificity in HIV-1 research

Multi-antibody Concordance Testing:

• Test multiple antibodies targeting different FNBP1L epitopes

• Compare staining patterns and signal localization

• Consistent detection across antibodies suggests specificity

Recombinant Protein Controls:

• Test antibody against recombinant FNBP1L and related family members (e.g., FNBP1)

• Evaluate cross-reactivity

• Confirm molecular weight correspondence with expected targets

Mass Spectrometry Validation:

• Perform immunoprecipitation using the FNBP1L antibody

• Analyze precipitated proteins by mass spectrometry

• Confirm presence of FNBP1L peptides and absence of non-specific targets

When implementing these approaches, research has shown successful demonstration of specificity through peptide competition assays, where FNBP1L antibody signals in mouse brain tissue were effectively blocked by pre-incubation with the immunizing peptide . Additionally, in studies on HIV-1 infection in dendritic cells, knockdown validation confirmed antibody specificity by demonstrating corresponding reductions in detected protein levels .

How can FNBP1L antibodies be employed to investigate endocytosis mechanisms?

FNBP1L antibodies can be strategically deployed to investigate endocytosis mechanisms through multiple sophisticated approaches:

Co-localization Studies with Endocytic Markers:

• Perform dual immunofluorescence labeling of FNBP1L and established endocytosis markers (clathrin, caveolin, EEA1, Rab5)

• Use confocal microscopy to visualize spatial relationships

• Calculate Pearson's correlation coefficients to quantify co-localization

• This approach has revealed FNBP1L participation in specific endocytic pathways and compartments

Live-Cell Imaging of Endocytic Events:

• Generate cells expressing fluorescently-tagged FNBP1L (ensuring tag doesn't disrupt function)

• Combine with fluorescent cargo tracers (transferrin, dextran)

• Track FNBP1L recruitment during endocytic vesicle formation in real-time

• Measure temporal dynamics of FNBP1L association with forming endosomes

Immunoprecipitation to Identify Endocytic Complex Components:

• Use FNBP1L antibodies for co-immunoprecipitation from cell lysates

• Analyze protein complexes by Western blot or mass spectrometry

• Identify interaction partners that regulate endocytosis (e.g., dynamins, WASP, WIP)

• Map temporal assembly of these complexes during endocytosis stages

Functional Endocytosis Assays with FNBP1L Perturbation:

• Deplete FNBP1L using siRNA or CRISPR techniques

• Measure uptake of fluorescent tracers (FITC-dextran, pHrodo E. coli bioparticles)

• Quantify changes in endocytic capacity

• Research has shown FNBP1L depletion reduces phagocytosis and endocytic activity in dendritic cells

Super-resolution Microscopy Applications:

• Use FNBP1L antibodies compatible with STORM or PALM microscopy

• Visualize nanoscale organization of FNBP1L at endocytic sites

• Measure precise spatial relationships with membrane curvature components

The implementation of these approaches has revealed FNBP1L's critical role in coordinating membrane tubulation with actin cytoskeleton reorganization during endocytosis . Additionally, research using pHrodo E. coli bioparticles has demonstrated that FNBP1L knockdown significantly impairs phagocytic activity in dendritic cells, highlighting its functional importance in specific endocytic pathways .

What is the role of FNBP1L in cancer research and how can antibodies help elucidate these mechanisms?

FNBP1L antibodies serve as critical tools for investigating its emerging roles in cancer biology through multiple experimental strategies:

Expression Analysis Across Cancer Types:

• Apply FNBP1L antibodies in tissue microarrays spanning multiple cancer types

• Quantify expression levels relative to matched normal tissues

• Correlate expression with clinicopathological features and patient outcomes

• Data indicates differential FNBP1L expression patterns between cancer subtypes

Investigation of FNBP1L in Cancer Cell Signaling:

• Use FNBP1L antibodies to study interactions with oncogenic signaling pathways

• Analyze co-localization and co-immunoprecipitation with FAK, PI3K and AKT components

• Research has revealed that unlike its family member FNBP1, FNBP1L may not directly maintain constitutive FAK/PI3K/AKT survival signaling in certain cancers

• Compare FNBP1L-mediated signaling in normal versus malignant cells

Cell Motility and Invasion Assays:

• Analyze FNBP1L distribution during cancer cell migration using immunofluorescence

• Correlate localization with invasion front markers

• Measure changes in migration capacity following FNBP1L knockdown or overexpression

• Emerging evidence suggests FNBP1L involvement in malignant tumor invasion and metastasis processes

Cancer Therapy Response Monitoring:

• Evaluate FNBP1L expression changes following treatment with chemotherapeutics

• Determine whether FNBP1L serves as a resistance biomarker

• Investigate FNBP1L-mediated endocytosis of therapeutic agents

FNBP1L in Cancer Immunology:

• Study FNBP1L function in tumor-associated immune cells

• Investigate its role in antigen presentation and immune surveillance

• Research indicates FNBP1L may regulate endocytic processes in dendritic cells that influence immune responses

While FNBP1 has been directly implicated in cervical cancer cell survival by maintaining FAK/PI3K/AKT signaling , the specific roles of FNBP1L in cancer biology are still being elucidated. Antibody-based approaches allow researchers to distinguish between these related family members and determine their potentially distinct functions in cancer progression. The application of FNBP1L antibodies in multiparametric analyses with other cancer markers provides contextual understanding of its role in tumor microenvironments and potential as a therapeutic target.

How do researchers investigate the FNBP1L role in viral infection using antibodies?

Researchers employ FNBP1L antibodies to investigate its role in viral infections through multifaceted experimental approaches:

Viral Entry and Trafficking Studies:

• Perform time-course immunofluorescence co-localization of FNBP1L with viral particles

• Track virus internalization in relation to FNBP1L-positive compartments

• Quantify temporal dynamics of association during entry phases

• Research has revealed FNBP1L involvement in limiting HIV-1 entry in dendritic cells

Functional Manipulation Experiments:

• Generate FNBP1L knockdown cells using shRNA approaches

• Measure changes in viral infection efficiency

• Analyze viral replication kinetics in FNBP1L-depleted vs. control cells

• Studies show FNBP1L silencing increases HIV-1 infection rates in dendritic cells

Mechanistic Investigation of Antiviral Activity:

• Use FNBP1L antibodies for co-immunoprecipitation with viral proteins

• Identify direct protein-protein interactions

• Map domains involved in virus recognition or restriction

• Determine whether interactions are direct or mediated through endocytic complexes

Endosomal Function Analysis:

• Combine FNBP1L antibody staining with endosomal acidification markers

• Assess if FNBP1L regulates pH-dependent viral uncoating processes

• Utilize pHrodo-labeled particles to measure endosomal acidification

• Research demonstrates FNBP1L knockdown impairs phagocytosis and endocytic activities in dendritic cells

Imaging of Virus-Host Membrane Interactions:

• Apply super-resolution microscopy with FNBP1L antibodies

• Analyze nanoscale organization at virus entry sites

• Visualize membrane remodeling during viral invasion attempts

Research using these approaches has demonstrated that shRNA-mediated knockdown of FNBP1L in monocyte-derived dendritic cells (MDDCs) significantly increases HIV-1 infection rates, suggesting FNBP1L normally restricts viral entry . Further investigation revealed FNBP1L depletion impairs endocytic and phagocytic activities, potentially altering the cellular entry mechanisms used by HIV-1. This indicates FNBP1L may function as part of the innate immune system's antiviral defense by regulating endocytic pathways that viruses exploit for entry . These findings provide new insights into potential targets for antiviral strategies specifically targeting early infection events.

What are common pitfalls when using FNBP1L antibodies and how can they be overcome?

Researchers working with FNBP1L antibodies commonly encounter several technical challenges that can be addressed through systematic troubleshooting:

High Background in Immunostaining:

Inconsistent Western Blot Detection:

Cell-Type Specific Challenges:

Validation and Controls:

• Always include positive control tissues (mouse brain shows reliable detection)

• Run parallel negative controls (omit primary antibody)

• Include genetic knockdown controls when possible

• Conduct peptide competition assays to confirm specificity

Alternative Detection Strategies:

• If one application fails (e.g., IHC), try alternative methods (IF, WB)

• Consider fixation-insensitive epitopes when designing experiments

• Use multiple antibodies targeting different FNBP1L epitopes to cross-validate

Research has demonstrated successful detection of FNBP1L in human brain tissue using antibodies at 2.5 μg/ml concentration , while peptide competition assays in mouse brain tissue confirmed specificity through signal elimination when antibody was pre-incubated with blocking peptide . When investigating FNBP1L in new tissues or applications, begin with validated protocols and systematically optimize each parameter while maintaining appropriate controls.

How should researchers interpret contradictory findings when studying FNBP1L expression and function?

When researchers encounter contradictory findings regarding FNBP1L expression or function, a systematic analytical framework helps resolve discrepancies:

Technical vs. Biological Variability Assessment:

• Antibody-Related Discrepancies:

  • Compare epitope targets between studies (N-terminal vs. C-terminal)

  • Evaluate antibody validation methodology and specificity controls

  • Consider isoform-specific recognition capabilities

  • Assess whether post-translational modifications affect epitope recognition

• Model System Differences:

  • Analyze cell type-specific FNBP1L expression patterns

  • Compare primary cells vs. immortalized cell lines

  • Consider species differences in FNBP1L function between human, mouse, and rat models

  • Evaluate developmental stage-specific expression patterns

• Contextual Analysis Framework:

• Functional Assay Harmonization:

  • Standardize functional readouts between studies

  • Compare endocytosis assay methodologies when interpreting FNBP1L function

  • Research has shown different endocytic markers (FITC-dextran vs. pHrodo E. coli bioparticles) may yield different results

• Integrative Data Analysis:

  • Combine protein-level (antibody) data with transcript-level evidence

  • Correlate FNBP1L expression with known functional markers

  • Perform pathway analysis to contextualize contradictory findings

When addressing contradictions between studies, consider that FNBP1L appears to have context-dependent functions. For example, research has shown its distinct roles in different cell types - while it limits HIV-1 infection in dendritic cells , its family member FNBP1 maintains FAK/PI3K/AKT survival signaling in cancer cells . These functional differences could explain seemingly contradictory findings across different experimental systems and highlight the importance of precisely defining the cellular context when reporting FNBP1L function.

What quantitative approaches can be used to analyze FNBP1L localization and protein interactions?

Advanced quantitative methods for analyzing FNBP1L localization and interactions enable precise characterization of its cellular functions:

Subcellular Localization Analysis:

• Colocalization Coefficient Calculation:

  • Calculate Pearson's correlation coefficient between FNBP1L and organelle markers

  • Determine Manders' overlap coefficients for partial colocalization scenarios

  • Use object-based colocalization for discrete structures

  • Apply these metrics to quantify FNBP1L association with membrane and cytoplasmic compartments

• Super-resolution Distribution Analysis:

  • Measure nearest-neighbor distances between FNBP1L and interacting proteins

  • Perform cluster analysis to identify FNBP1L-enriched microdomains

  • Quantify molecule density at endocytic sites

• Dynamic Redistribution Measurements:

  • Track FNBP1L relocalization during endocytosis using time-lapse microscopy

  • Calculate fluorescence recovery after photobleaching (FRAP) to measure mobility

  • Determine residence time at membrane domains

Protein-Protein Interaction Quantification:

• Co-immunoprecipitation Analysis:

  • Use FNBP1L antibodies to pull down protein complexes

  • Quantify interaction strength through densitometry

  • Compare interaction profiles across different cellular conditions

  • This approach has helped identify FNBP1L interactions with components like WASP, WIP and dynamin-2

• Proximity Ligation Assay (PLA):

  • Quantify in situ protein-protein interactions at single-molecule resolution

  • Measure interaction distances within 40nm range

  • Calculate PLA signals per cell to determine interaction frequency

• FRET/BRET Analysis:

  • Measure direct protein interactions through energy transfer

  • Calculate FRET efficiency to determine proximity

  • Perform acceptor photobleaching to confirm specificity

Systems-level Interaction Analysis:

Image Analysis Automation:

• Develop machine learning algorithms to segment and quantify FNBP1L-positive structures

• Apply high-content screening approaches for phenotypic analysis

• Implement tracking algorithms to follow FNBP1L-associated vesicles

These quantitative approaches have revealed that FNBP1L localizes primarily to the cell membrane, cytoplasmic vesicles, and cytoplasm , with dynamic redistribution during endocytic events. Interaction studies have confirmed its associations with components of the actin polymerization machinery through its SH3 domain . When FNBP1L is depleted in dendritic cells, quantitative analysis of pHrodo E. coli bioparticle uptake demonstrates significantly reduced integrated fluorescence intensity, indicating impaired phagocytic activity . This multidimensional quantitative approach provides comprehensive characterization of FNBP1L's functional roles in cellular processes.

How is FNBP1L being investigated in the context of infectious disease research beyond HIV?

FNBP1L is emerging as a critical factor in host-pathogen interactions beyond HIV, with several investigative directions utilizing antibody-based approaches:

Broad-Spectrum Antiviral Activity Assessment:

• Apply FNBP1L antibodies to track distribution during infection with diverse viral families

• Compare colocalization patterns with different viral entry mechanisms

• Quantify FNBP1L recruitment to viral entry sites across pathogen types

• Building on HIV studies , researchers are exploring if FNBP1L restriction extends to other enveloped viruses

Bacterial Pathogenesis Studies:

• Investigate FNBP1L distribution during bacterial invasion

• Analyze interaction with bacterial effector proteins

• Monitor phagosome maturation in FNBP1L-depleted cells

• Research using pHrodo E. coli bioparticles demonstrated FNBP1L's role in phagocytic activity , suggesting broader antibacterial functions

Pathogen-Induced Membrane Remodeling:

• Track FNBP1L during pathogen-induced membrane deformation

• Study competitive dynamics between pathogen factors and FNBP1L

• Visualize membrane curvature changes during infection

• Since FNBP1L coordinates membrane tubulation during endocytosis , it may compete with microbial factors targeting similar processes

Immune Cell Function Analysis:

• Compare FNBP1L dynamics across multiple immune cell types (dendritic cells, macrophages, neutrophils)

• Correlate FNBP1L expression with antimicrobial activity

• Assess impact on antigen presentation capabilities

• Building on findings in dendritic cells , researchers are expanding to other immune cell lineages

Potential Therapeutic Applications:

• Screen for compounds that enhance FNBP1L antiviral activity

• Develop peptide mimetics of FNBP1L functional domains

• Assess FNBP1L activity modulation as anti-infective strategy

Recent research has demonstrated that silencing FNBP1L in monocyte-derived dendritic cells enhances HIV-1 infection while impairing phagocytic and endocytic activities . This suggests FNBP1L might function as a restriction factor controlling entry pathways exploited by diverse pathogens. As a membrane tubulation regulator , FNBP1L potentially influences the success of any pathogen requiring endocytic uptake. Investigating these mechanisms may identify new therapeutic targets that leverage natural host restriction factors against multiple infectious agents.

What are the latest technical advances in FNBP1L antibody-based research methods?

Recent technical innovations have significantly enhanced FNBP1L antibody-based research capabilities:

Advanced Imaging Approaches:

• Lattice Light-Sheet Microscopy:

  • Captures rapid 3D dynamics of FNBP1L during endocytosis

  • Reduces phototoxicity for extended live imaging

  • Enables visualization of transient membrane interactions

  • Particularly valuable for tracking FNBP1L's role in membrane tubulation events

• Super-Resolution Expansion Microscopy:

  • Physically expands specimens to achieve nanoscale resolution

  • Allows precise mapping of FNBP1L nanodomain organization

  • Compatible with standard FNBP1L antibodies

  • Enhances visualization of FNBP1L-membrane interactions

• Correlative Light and Electron Microscopy (CLEM):

  • Combines FNBP1L immunofluorescence with ultrastructural analysis

  • Precisely localizes FNBP1L to membrane curvature events

  • Provides nanometer-resolution context for FNBP1L function

Multiplexed Detection Systems:

• Mass Cytometry (CyTOF):

  • Simultaneously analyzes dozens of parameters including FNBP1L

  • Uses metal-tagged antibodies for high-dimensional analysis

  • Enables comprehensive signaling pathway mapping

  • Contextualizes FNBP1L within broader cellular networks

• Multiplexed Immunofluorescence:

  • Sequential staining with spectral unmixing

  • Allows simultaneous detection of FNBP1L with multiple interaction partners

  • Provides contextualized data on complex formation

• Spatial Transcriptomics Integration:

  • Combines FNBP1L protein detection with local transcriptome analysis

  • Correlates protein localization with gene expression patterns

  • Provides multimodal insight into FNBP1L regulation

Novel Interaction Analysis Methods:

Antibody Engineering Advances:

• Nanobody development against FNBP1L functional domains for improved accessibility

• Site-specific antibody conjugation for precise fluorophore positioning

• Bispecific antibodies targeting FNBP1L and interaction partners simultaneously

These technological advances enhance researchers' ability to study FNBP1L's role in coordinating membrane tubulation with actin cytoskeleton reorganization during endocytosis , its participation in limiting HIV-1 infection in dendritic cells , and its potential roles in cancer biology. The implementation of these approaches will provide unprecedented insight into the dynamic behavior and functional interactions of FNBP1L in diverse cellular contexts.

How does FNBP1L research contribute to understanding fundamental cellular processes?

FNBP1L research contributes to our understanding of fundamental cellular processes through multiple interconnected mechanisms:

Membrane-Cytoskeleton Interface Regulation:

• FNBP1L serves as a critical mediator between membrane remodeling and actin dynamics

• Its F-BAR domain senses and induces membrane curvature while the SH3 domain recruits actin regulators

• This coordination is essential for processes beyond endocytosis, including cell migration, division, and organelle shaping

• Antibody-based studies reveal spatial coordination of these events in diverse cell types

Endocytic Pathway Specialization:

• FNBP1L contributes to the diversification of endocytic mechanisms

• Research shows its differential involvement across clathrin-dependent and independent pathways

• Experimental depletion of FNBP1L in dendritic cells impairs both FITC-dextran uptake and pHrodo E. coli bioparticle phagocytosis

• This suggests cell-type specific roles in specialized endocytic functions

Cell Type-Specific Adaptations:

• FNBP1L expression patterns vary across tissues and cell types

• Antibody-based detection reveals differential subcellular localization patterns

• Functional consequences include specialized endocytic capacities in immune cells

• This contributes to understanding cellular diversity and specialization

Signaling Network Integration:

• FNBP1L participates in complex signaling networks

• Unlike its family member FNBP1, it may not directly maintain FAK/PI3K/AKT survival signaling in certain contexts

• Research reveals context-dependent interaction with signaling pathways

• This illuminates how membrane dynamics interface with cellular signaling

Innate Immunity Mechanisms:

• FNBP1L's role in limiting HIV-1 infection highlights its function in cellular defense

• Knockdown experiments demonstrate increased viral infection in dendritic cells when FNBP1L is depleted

• This reveals how fundamental cellular machinery can be repurposed for pathogen defense

• Contributes to understanding the evolutionary relationship between endocytosis and immunity

Developmental and Disease Implications: