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GeneE
25 sources retrieved Β· Most recent: April 2026 Β· Index updated 14 days ago
β“˜GeneE is for informational purposes only. It is not a substitute for professional medical advice, diagnosis, or treatment.
GSN
gelsolin
Chromosome 9 Β· 9q33.2
NCBI Gene: 2934Ensembl: ENSG00000148180.22HGNC: HGNC:4620UniProt: A0A0A0MS51
373PubMed Papers
21Diseases
0Drugs
6Pathogenic Variants
FUNCTIONAL ROLE
Hub Gene
RESEARCH IMPACT
Highly StudiedTrending
CLINICAL
OMIM Disease Gene
DATA QUALITY
βœ“ Experimental GO Evidenceβœ“ Swiss-Prot Reviewed
cortical actin cytoskeletonamyloid fibril formationGO:0005615actin cytoskeletonFinnish type amyloidosisFamilial amyloidosis, Finnish typeAL amyloidosiscardiomyopathy
✦AI Summary

Gelsolin (GSN) is a calcium-regulated actin-binding protein that functions as a multifaceted cytoskeletal regulator with emerging roles in inflammatory and cardiovascular disease. Primary functions include actin filament capping, severing, and nucleation activities that organize the cytoskeleton 1. GSN also participates in ciliogenesis 2. Mechanistically, GSN regulates actin dynamics through calcium-dependent binding to actin filament barbed ends. Beyond cytoskeletal roles, GSN negatively regulates NLRP3 inflammasome activation in macrophages by interacting with NLRP3 and preventing its mitochondrial translocation, thereby maintaining intracellular calcium equilibrium and mitochondrial stability 3. In cardiac pathophysiology, GSN is a direct target of NAE1 (NEDD8-activating enzyme), where increased NAE1 crotonylation promotes GSN neddylation and protein stability, enhancing GSN's actin-severing activity and driving pathological cardiac hypertrophy and cytoskeletal remodeling 4. Disease relevance includes hereditary systemic amyloidosis (Finnish type), associated with GSN mutations 5. Notably, plasma GSN levels are significantly reduced in rheumatoid arthritis patients, and GSN-deficient mice exhibit exacerbated arthritic symptoms and enhanced inflammatory responses across multiple disease models including sepsis and acute kidney injury 3. These findings establish GSN as both a diagnostic biomarker and therapeutic target for inflammatory and cardiovascular diseases.

Sources cited
1
GSN binds actin filaments and promotes nucleation, severing, and capping activities
PMID: 19666512
2
GSN plays a role in ciliogenesis
PMID: 20393563
3
GSN negatively regulates NLRP3 inflammasome activation, is reduced in RA patient plasma, and its deficiency exacerbates inflammatory disease
PMID: 39179640
4
NAE1 crotonylation promotes GSN neddylation and stability, enhancing actin-severing activity and driving pathological cardiac hypertrophy
PMID: 39229723
5
GSN mutations are associated with hereditary systemic amyloidosis, Finnish type, a form of early-onset cerebral amyloid angiopathy
PMID: 37280119
Disease Associationsβ“˜21
Finnish type amyloidosisOpen Targets
0.80Strong
Familial amyloidosis, Finnish typeOpen Targets
0.77Strong
AL amyloidosisOpen Targets
0.46Moderate
cardiomyopathyOpen Targets
0.42Moderate
cutis laxaOpen Targets
0.42Moderate
peripheral neuropathyOpen Targets
0.42Moderate
cranial nerve neuropathyOpen Targets
0.42Moderate
ArrhythmiaOpen Targets
0.42Moderate
cardiac arrhythmiaOpen Targets
0.42Moderate
genetic disorderOpen Targets
0.42Moderate
cervical carcinomaOpen Targets
0.28Weak
alcohol drinkingOpen Targets
0.24Weak
amyloidosisOpen Targets
0.19Weak
gastric cancerOpen Targets
0.10Suggestive
breast cancerOpen Targets
0.10Suggestive
Alzheimer diseaseOpen Targets
0.09Suggestive
glioblastoma multiformeOpen Targets
0.09Suggestive
cancerOpen Targets
0.09Suggestive
SepsisOpen Targets
0.09Suggestive
hepatocellular carcinomaOpen Targets
0.09Suggestive
Amyloidosis, hereditary systemic 4, Finnish typeUniProt
Pathogenic Variants6
NM_198252.3(GSN):c.487G>A (p.Asp163Asn)Pathogenic
Finnish type amyloidosis|not provided|Inborn genetic diseases
β˜…β˜…β˜†β˜†2026β†’ Residue 163
NM_198252.3(GSN):c.480C>A (p.Asn160Lys)Pathogenic
not provided|Finnish type amyloidosis
β˜…β˜…β˜†β˜†2024β†’ Residue 160
NM_198252.3(GSN):c.487G>T (p.Asp163Tyr)Pathogenic
Finnish type amyloidosis|not provided
β˜…β˜…β˜†β˜†2023β†’ Residue 163
NM_198252.3(GSN):c.-9-1987dupLikely pathogenic
Finnish type amyloidosis
β˜…β˜†β˜†β˜†
NM_198252.3(GSN):c.1267T>C (p.Tyr423His)Pathogenic
Finnish type amyloidosis
β˜†β˜†β˜†β˜†β†’ Residue 423
NM_198252.3(GSN):c.749A>G (p.Tyr250Cys)Pathogenic
Finnish type amyloidosis
β˜†β˜†β˜†β˜†β†’ Residue 250
View on ClinVar β†—
Related Genes
VASPProtein interaction100%TLN2Protein interaction100%TLN1Protein interaction100%PXNProtein interaction100%APOEProtein interaction100%FLNAProtein interaction100%
Tissue Expression6 tissues
Heart
100%
Lung
26%
Ovary
23%
Bone Marrow
19%
Brain
13%
Liver
4%
Gene Interaction Network
Click a node to explore
GSNVASPTLN2TLN1PXNAPOEFLNA
PROTEIN STRUCTURE
Preparing viewer…
PDB5FAF Β· 1.05 Γ… Β· X-ray
View on RCSB β†—
Constraintβ“˜
LOEUFβ“˜
0.79LoF Tolerant
pLIβ“˜
0.00Tolerant
Observed/Expected LoF0.62 [0.48–0.79]
RankingsWhere GSN stands among ~20K protein-coding genes
  • #816of 20,598
    Most Researched373 Β· top 5%
  • #3,295of 5,498
    Most Pathogenic Variants6
  • #6,495of 17,882
    Most Constrained (LOEUF)0.79
Genes detectedGSN
Sources retrieved25 papers
Response timeβ€”
πŸ“„ Sources
25β–Ό
1
Crotonylation of NAE1 Modulates Cardiac Hypertrophy via Gelsolin Neddylation.
PMID: 39229723
Circ Res Β· 2024
1.00
2
Spatial proteomics in three-dimensional intact specimens.
PMID: 36563667
Cell Β· 2022
0.90
3
Clinical considerations in early-onset cerebral amyloid angiopathy.
PMID: 37280119
Brain Β· 2023
0.80
4
Cellular and Molecular Probing of Intact Human Organs.
PMID: 32059778
Cell Β· 2020
0.70
5
Phase Separation of FUS Is Suppressed by Its Nuclear Import Receptor and Arginine Methylation.
PMID: 29677514
Cell Β· 2018
0.68