Flotillin-2 (also known as Reggie-1) is a 43 kDa integral membrane protein belonging to the flotillin family. Along with flotillin-1, flotillin-2 organizes lipid raft microdomains and participates in various cellular processes including signal transduction, membrane trafficking, and cell adhesion. In the nervous system, flotillin-2 is expressed in neurons and glial cells where it regulates synaptic function and has been implicated in neurodegenerative processes.
| Flotillin-2 | |
|---|---|
| Protein Name | Flotillin-2 |
| Gene | FLOT2 |
| UniProt ID | Q14244 |
| PDB Structures | 2MAU |
| Molecular Weight | 43 kDa |
| Subcellular Localization | Membrane rafts, Cytoplasm |
| Protein Family | Flotillin family |
Flotillin-2 is a member of the reggie/flotillin protein family that was originally identified in neurons as proteins upregulated during optic nerve regeneration. Flotillin proteins form hetero-oligomeric complexes that localize to lipid rafts and participate in various signaling pathways. In the brain, flotillin-2 is involved in synaptic vesicle trafficking, neurotransmitter release, and neuronal signaling.
The FLOT2 gene encodes flotillin-2, which is widely expressed in various tissues including the brain. Flotillin-2 functions as a scaffold protein that clusters signaling molecules in lipid rafts, facilitating efficient signal transduction. Research has shown that flotillin-2 participates in pathways relevant to neurodegeneration including amyloid-beta signaling and neuroinflammation. The protein's role in membrane trafficking and its presence at synapses make it relevant to understanding synaptic dysfunction in Alzheimer's Disease and related disorders.
Flotillin-2 is a 43 kDa protein belonging to the Flotillin family.
Flotillin-2 is a lipid raft-associated scaffold protein involved in signal transduction, membrane trafficking, and synaptic function. It organizes protein complexes at membrane microdomains.
Flotillin-2 in neurodegeneration:
Modulates amyloid-beta toxicity
Involved in neuroinflammation
Altered in Alzheimer's Disease brains
Alzheimer's Disease, Cancer
Further research is needed to identify key publications for this protein.