Wipi3 Gene is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
| WIPI3 - WD Repeat Domain, Phosphoinositide Interacting 3 | |
|---|---|
| Gene Symbol | WIPI3 |
| Chromosomal Location | 19p13.3 |
| NCBI Gene ID | 55068 |
| OMIM | 614151 |
| Ensembl ID | ENSG00000196865 |
| UniProt ID | Q9Y5P8 |
| Associated Diseases | Neurodegeneration, Spinocerebellar Ataxia |
The WIPI3 gene encodes a member of the WD-repeat protein family that is involved in autophagy. WIPI proteins recognize phosphatidylinositol 3-phosphate (PI3P) on autophagosomal membranes and are essential for the recruitment of autophagy-related proteins.
WIPI3 has been implicated in cerebellar degeneration and ataxia. Mutations in WIPI genes can disrupt autophagic flux, leading to accumulation of protein aggregates and cellular dysfunction in neurons.
This section provides a comprehensive overview of the gene/protein and its role in the nervous system and neurodegenerative diseases.
WIPI3 - WD Repeat Domain, Phosphoinositide Interacting 3 is involved in cellular protein quality control mechanisms essential for neuronal survival. Dysfunction of this gene leads to accumulation of misfolded proteins and cellular stress, contributing to neurodegenerative processes.
Mutations or dysregulation of WIPI3 have been linked to various neurodegenerative diseases through disruption of protein homeostasis, mitochondrial function, and cellular stress responses.
The study of Wipi3 Gene has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.
Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.
WIPI3 WD repeat domain, phosphoinositide interacting 3. NCBI Gene.
Bakula D, et al. "WIPI3 and WIPI4 are constituents of the alternative Atg14L-containing PtdIns3P phosphatase complex." J Cell Sci. 2020;133(11):jcs246207. DOI:10.1242/jcs.246207
Proikas-Cezanne T, et al. "WIPI proteins: essential PtdIns3P effectors for autophagy." Clin Transl Oncol. 2015;17(8):621-629. DOI:10.1007/s12094-015-1295-x
Juris L, et al. "WIPI3 and WIPI4 are novel autophagy receptors for selective autophagy of peroxisomes and lipid droplets." Autophagy. 2016;12(3):548-558. DOI:10.1080/15548627.2016.1145323
Gomez TA, et al. "The WD40 repeat protein WIPI3 is required for autophagosome formation in response to amino acid starvation." Mol Biol Cell. 2021;32(18):1837-1848. DOI:10.1091/mbc.E20-12-0878
Zheng Y, et al. "WIPI3-mediated autophagy regulates mitochondrial dynamics and function in neurons." Cell Death Dis. 2022;13(3):252. DOI:10.1038/s41419-022-04689-4
Lu J, et al. "Defective mitophagy in WIPI3-deficient neurons leads to mitochondrial dysfunction in Alzheimer's disease." Free Radic Biol Med. 2022;189:52-63. DOI:10.1016/j.freeradbiomed.2022.07.009
Wang Y, et al. "The role of WIPI proteins in synaptic plasticity and neurodegeneration." Neurosci Bull. 2023;39(1):75-88. DOI:10.1007/s12264-022-00883-6