NUP62CL interacts with core nucleoporins to maintain NPC integrity and regulate bidirectional transport of proteins and RNA . Key functional partners include:
Interacting Protein | Role in NPC | Interaction Score |
---|---|---|
NUP54 | Component of the NPC scaffold | 0.979 |
NUP93 | Anchors nucleoporins to the NPC core | 0.911 |
NUP107 | Required for NPC assembly and maintenance | 0.860 |
NUP62CL’s C-terminal domain is critical for recruiting peripheral nucleoporins to the NPC, ensuring proper transport of cargo molecules .
NUP62CL has emerged as a prognostic biomarker in LUAD, with implications for telomere maintenance and immune infiltration:
Gene Set Enrichment Analysis (GSEA) revealed overrepresentation of pathways linked to:
NUP62CL is widely expressed, with notable abundance in:
Tissue/Organ | Expression Level | Source |
---|---|---|
Brain | High | Human Protein Atlas , Abcam |
Liver | High | Abcam |
Kidney | Moderate | Abcam |
Lung (Tumor) | Elevated in LUAD | HPA |
Immunohistochemistry data confirm cytoplasmic and nuclear localization in normal and cancerous tissues .
The NUP62CL gene harbors 16 reported variants, primarily benign or of uncertain significance . No pathogenic variants are strongly linked to diseases, though associations with mental retardation have been explored .
NUP62CL encodes a protein containing domains found in nucleoporins, which are essential components of nuclear pore complexes (NPCs). These complexes regulate molecular transport between the nucleus and cytoplasm. According to the gene description, alternative splicing results in multiple transcript variants . As a nucleoporin family member, NUP62CL likely contributes to nucleocytoplasmic transport regulation, though its specific role may differ from canonical nucleoporins.
Methodologically, researchers investigating NUP62CL function should consider:
Subcellular localization studies using fluorescent protein tagging or immunocytochemistry
Protein-protein interaction analyses with other nuclear pore complex components
Loss-of-function experiments via RNA interference or CRISPR-Cas9
Rescue experiments with wild-type or mutant constructs to validate phenotypes
NUP62CL expression has been studied across multiple tissue types and developmental stages as evidenced by its inclusion in numerous expression databases:
Database | Type of Expression Data |
---|---|
Allen Brain Atlas Adult Human Brain | Brain region-specific expression |
Allen Brain Atlas Developing Human Brain | Developmental expression in brain tissues |
BioGPS Human Cell Type and Tissue | Expression across diverse cell types |
GTEx Tissue Gene Expression Profiles | Systematic tissue expression patterns |
CCLE Cell Line Gene Expression | Expression across cancer cell lines |
Researchers can leverage these resources to identify tissues with high or low NUP62CL expression . Brain tissues appear to be of particular interest given the multiple brain-specific expression datasets containing NUP62CL data.
To validate expression patterns, researchers should employ:
qRT-PCR across tissue panels
Western blotting with validated antibodies
Single-cell RNA sequencing for cellular resolution
In situ hybridization for spatial context within tissues
Transcriptional regulation of NUP62CL can be investigated through multiple approaches. Based on the Harmonizome database listings, NUP62CL appears in several transcription factor datasets:
CHEA Transcription Factor Binding Site Profiles
ENCODE Transcription Factor Binding Site Profiles
These resources suggest that specific transcription factors may bind to the NUP62CL promoter region, and that histone modifications likely play a role in its expression regulation.
Recommended methodological approaches include:
Chromatin immunoprecipitation (ChIP) to identify bound transcription factors
Reporter gene assays with promoter constructs
CRISPR-based epigenome editing to modulate specific regulatory elements
DNase hypersensitivity assays to identify open chromatin regions
As a protein containing nucleoporin domains, NUP62CL likely participates in nuclear pore complex (NPC) formation. Advanced experimental approaches should include:
Proximity labeling techniques:
BioID or TurboID fusion proteins to identify proteins in close proximity to NUP62CL
APEX2 proximity labeling for temporal control of labeling reactions
Analysis of labeled proteins by mass spectrometry
Live-cell imaging approaches:
Fluorescence Recovery After Photobleaching (FRAP) to study dynamics
Single-particle tracking to monitor movement within the NPC
Super-resolution microscopy (STORM, PALM) for detailed localization
In vitro reconstitution:
Purification of recombinant NUP62CL and potential interacting partners
Electron microscopy of reconstituted subcomplexes
Biochemical assays to assess complex formation and stability
The cellular compartments containing NUP62CL protein can be revealed through analysis of the COMPARTMENTS Curated Protein Localization Evidence Scores dataset , providing guidance for experimental design.
Disease associations for NUP62CL can be found in:
To study the functional impact of disease-associated mutations:
Structural analysis approaches:
Homology modeling of NUP62CL domains
Molecular dynamics simulations to predict mutation effects
In silico mutagenesis and stability predictions
Functional characterization:
Site-directed mutagenesis to introduce disease-associated variants
Complementation assays in knockout/knockdown cells
Protein interaction studies comparing wild-type and mutant forms
Nucleocytoplasmic transport assays with reporter constructs
Disease model development:
Patient-derived cell lines harboring mutations
CRISPR-engineered isogenic cell lines
Animal models with orthologous mutations
When analyzing disease associations, researchers should ensure careful validation of genotype-phenotype correlations and consider potential confounding factors.
Nucleoporins often play critical roles in cell division and cell cycle regulation. To investigate NUP62CL's potential role:
Cell synchronization experiments:
Serum starvation/release protocols
Double thymidine block for S-phase synchronization
Nocodazole treatment for mitotic arrest
Analysis of NUP62CL expression and localization across cell cycle phases
Live-cell imaging approaches:
Time-lapse microscopy with fluorescently tagged NUP62CL
Correlation with cell cycle markers
Quantitative image analysis of nuclear envelope dynamics
Perturbation studies:
Cell cycle analysis after NUP62CL depletion or overexpression
Rescue experiments with cell cycle-regulated variants
Combined perturbation with cell cycle regulators
The CMAP and GEO Signatures datasets may contain information about how chemical perturbations affecting cell cycle also impact NUP62CL expression .
Post-translational modifications (PTMs) often regulate nucleoporin function:
PTM identification strategies:
Mass spectrometry analysis of immunoprecipitated NUP62CL
Phospho-specific antibodies for common modifications
PTM-specific enrichment techniques (e.g., TiO₂ for phosphopeptides)
Functional analysis of PTMs:
Site-directed mutagenesis of modified residues
Phosphomimetic mutations (e.g., Ser→Asp) or phospho-null mutations (e.g., Ser→Ala)
Cell cycle-dependent analysis of modifications
Kinase/phosphatase inhibitor treatments
Enzymes responsible for modifications:
Kinase prediction algorithms
In vitro kinase assays
Targeted knockdown of candidate modifying enzymes
Building a comprehensive PTM map will help understand how NUP62CL is dynamically regulated in different cellular contexts.
Developing specific antibodies for NUP62CL research requires careful planning:
Epitope selection considerations:
Analyze sequence similarity with other nucleoporins, especially NUP62
Target unique regions to avoid cross-reactivity
Consider accessibility in the native protein conformation
Evaluate potential post-translational modification sites
Validation strategies:
Western blotting with overexpression and knockout controls
Immunoprecipitation followed by mass spectrometry
Immunofluorescence with siRNA knockdown controls
Peptide competition assays
Application-specific optimization:
Fixation conditions for immunohistochemistry
Detergent selection for nuclear envelope proteins
Blocking conditions to reduce background
When commercial antibodies are unavailable or unsatisfactory, epitope tagging approaches (FLAG, HA, etc.) offer alternatives for detection in experimental systems.
The DepMap CRISPR Gene Dependency dataset contains information about how cancer cell lines respond to NUP62CL knockout :
Bioinformatic analysis approaches:
Mining DepMap and other dependency databases for NUP62CL patterns
Correlation with genomic features (mutations, CNVs, expression)
Cell line clustering based on dependency profiles
Experimental validation methods:
CRISPR knockout in selective cell line panels
shRNA knockdown with multiple constructs
Growth, survival, and phenotypic assays
Complementation with wild-type or mutant constructs
Data interpretation framework:
Distinguishing context-dependent from general dependencies
Correlation with NUP62CL expression levels (CCLE data)
Integration with copy number variation data (COSMIC, CCLE)
Analysis of potential synthetic lethal interactions
The COSMIC Cell Line Gene CNV Profiles and CCLE Cell Line Gene CNV Profiles datasets provide additional information about NUP62CL copy number variations across cancer cell lines.
The gene description indicates that alternative splicing results in multiple transcript variants of NUP62CL . Researchers should address this complexity through:
Transcript identification strategies:
RNA-Seq analysis with junction-spanning reads
PCR with primers flanking alternative exons
5' and 3' RACE to capture all transcript ends
Long-read sequencing (PacBio, Nanopore) for full-length isoforms
Isoform-specific experimental design:
PCR primers targeting unique exon junctions
siRNAs targeting specific variants
Expression constructs for individual isoforms
Antibodies recognizing shared or unique epitopes
Functional comparison methods:
Rescue experiments with different isoforms
Localization studies of individual variants
Interaction partner analysis for each isoform
Temporal and spatial expression pattern analysis
A comprehensive isoform catalog should be established before undertaking detailed functional studies to ensure biological relevance.
The Harmonizome database indicates that NUP62CL appears in numerous datasets spanning different biological data types . Effective integration requires:
Data integration strategies:
Network-based approaches linking transcriptomic, proteomic, and genetic data
Pathway enrichment analysis across multiple data types
Correlation analysis between expression and functional readouts
Machine learning approaches to identify patterns across datasets
Recommended computational resources:
Cytoscape for network visualization and analysis
R packages for multi-omics integration (mixOmics, MultiAssayExperiment)
Galaxy workflows for reproducible analysis pipelines
Database query tools for mining existing datasets
Validation and interpretation frameworks:
Hypothesis generation from integrated data
Targeted experimental validation of computational predictions
Iterative refinement of models based on new data
Context-specific interpretation considering cell type and condition
The comprehensive list of datasets containing NUP62CL information provides a valuable starting point for multi-omics integration efforts .
Scientific literature often contains seemingly contradictory results, which may stem from:
Sources of contradiction:
Different experimental systems (cell lines, tissues, organisms)
Varied technical approaches and sensitivity
Context-dependent functions of NUP62CL
Isoform-specific effects not accounted for
Antibody cross-reactivity issues
Resolution strategies:
Systematic comparison of experimental conditions
Direct replication studies with controlled variables
Meta-analysis of published findings
Development of unified models accounting for context-dependency
Experimental design recommendations:
Include multiple complementary approaches
Test findings across different cell types or tissues
Control for expression of specific isoforms
Use genetic rescue experiments to confirm specificity
Report detailed methodological information to facilitate replication
When evaluating chemical interaction effects, researchers should consult the CTD Gene-Chemical Interactions dataset to understand how different compounds may influence NUP62CL expression or function.
The GEO Signatures of Differentially Expressed Genes for Viral Infections dataset contains information about how viral infections affect NUP62CL expression :
Investigation approaches:
Analysis of NUP62CL expression changes during infection
Localization studies in infected versus uninfected cells
Protein-protein interaction studies with viral components
Loss-of-function studies to assess viral replication effects
Mechanistic considerations:
Role in viral nuclear import/export
Potential viral targeting of nuclear pore complex
Involvement in antiviral signaling pathways
Subversion mechanisms employed by viruses
Therapeutic implications:
Potential as antiviral target
Biomarker for specific viral infections
Role in determining cell type tropism
Understanding NUP62CL's role in viral infections could provide insights into both basic virology and potential therapeutic approaches.
Despite sharing domains with other nucleoporins, NUP62CL likely has unique functions:
Comparative analysis approaches:
Sequence and structural comparisons with other nucleoporins
Phylogenetic analysis across species
Expression pattern comparisons
Interaction partner analysis
Functional differentiation methods:
Rescue experiments in cells depleted of different nucleoporins
Cargo specificity determination
Localization within the nuclear pore complex architecture
Response to cellular stresses or signaling events
Evolutionary considerations:
Analysis of selective pressures on different domains
Comparison of domain architecture across species
Investigation of lineage-specific functions
The "CL" (C-terminal like) designation suggests structural similarities with the C-terminal region of NUP62, but likely with functional divergence that merits detailed investigation.
NUP62CL is a small protein composed of 95 amino acids . It is non-glycosylated, meaning it does not have carbohydrate groups attached to it. The protein is involved in various cellular processes, including the regulation of nucleocytoplasmic transport, which is essential for maintaining cellular homeostasis and function.
NUP62CL shows close similarity to several other proteins, including:
NUP62CL is used in various research applications, particularly in the study of nucleocytoplasmic transport and the function of the NPC. It is also utilized in the development of antibodies for immunohistochemistry and other immunological techniques. The protein is available in different forms and quantities from various suppliers, such as ProSpec and RayBiotech .