| Protein Name | Annexin A11 |
|---|---|
| Gene | [ANXA11](/genes/anxa11) |
| UniProt ID | P50995 |
| Protein Size | 505 amino acids (~54 kDa) |
| Subcellular Localization | Cytoplasm; nucleus; plasma membrane; cytoskeleton |
| Protein Family | Annexin family (calcium-dependent phospholipid-binding proteins) |
| PDB Structures | 1HMH, 1XJL |
Annexin A11 (ANXA11) is a calcium-dependent phospholipid-binding protein that plays important roles in membrane organization, vesicle trafficking, and more recently has been implicated in the pathogenesis of ALS and other neurodegenerative diseases.
ANXA11 has a characteristic annexin domain structure:
The protein forms a convex surface with the convex face being the membrane-binding surface.
In normal cells, ANXA11 functions in:
Membrane Organization: Binds to phospholipid membranes in a calcium-dependent manner, helping organize membrane domains.
Vesicle Trafficking: Participates in endocytic and exocytic vesicle transport.
Cytoskeletal Interactions: Associates with actin cytoskeleton to regulate membrane-cytoskeleton dynamics.
Nuclear Functions: Can translocate to the nucleus where it may regulate gene expression.
Phagocytosis: Involved in macrophage phagocytosis of apoptotic cells.
ANXA11 was identified as an ALS susceptibility gene through GWAS[1]. Pathogenic mutations (e.g., D40G, R235C, G38R) disrupt the normal function of ANXA11 in several ways:
ANXA11 mutations have also been reported in FTD cases, suggesting a shared pathomechanism with ALS.
ANXA11 is upregulated in AD brains and may contribute to altered membrane dynamics and inflammation.
No specific ANXA11-targeted therapies exist yet, but strategies under investigation include:
ANXA11 interacts with: