WIPI1
Description
The WIPI1 (WD repeat domain, phosphoinositide interacting 1) is a protein-coding gene located on chromosome 17.
WD repeat domain phosphoinositide-interacting protein 1 (WIPI-1), also known as Atg18 protein homolog (ATG18) and WD40 repeat protein interacting with phosphoinositides of 49 kDa (WIPI 49 kDa), is a protein that in humans is encoded by the WIPI1 gene.
== Structure and function == WD40 repeat proteins are key components of many essential biologic functions. They regulate the assembly of multiprotein complexes by presenting a beta-propeller platform for simultaneous and reversible protein–protein interactions. Members of the WIPI subfamily of WD40 repeat proteins, such as WIPI1, have a 7-bladed propeller structure and contain a conserved motif for interaction with phospholipids.
== See also == WIPI protein family
== References ==
== Further reading ==
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
WIPI1 is a crucial component of the autophagy machinery, the process by which cells break down and recycle cellular components. It plays a vital role in both starvation-induced and calcium-mediated autophagy, as well as in mitophagy, the selective degradation of mitochondria. WIPI1 acts downstream of ULK1 and PI3-kinases, which are enzymes involved in the early stages of autophagy. It binds to phosphatidylinositol 3-phosphate (PtdIns3P), a signaling molecule that recruits WIPI1 to the endoplasmic reticulum where autophagosomes are formed. Once at this site, WIPI1 works with WIPI2 to attract ATG12-ATG5-ATG16L1, a complex essential for autophagosome elongation. Additionally, WIPI1 collaborates with WDR45/WIPI4 to promote the transfer of lipids by enhancing the interaction of ATG2 with membranes containing phosphatidylinositol 3-monophosphate (PI3P). WIPI1 also participates in xenophagy, the specific degradation of invading bacteria like Staphylococcus aureus. It is involved in the entrapment of these bacteria within autophagosome-like vesicles that are then targeted for lysosomal degradation. Beyond its role in autophagy, WIPI1 is implicated in the control of melanogenic enzyme transcription and melanosome maturation, a process distinct from starvation-induced autophagy. It may also regulate protein trafficking in the mannose-6-phosphate receptor (MPR) recycling pathway.
WIPI1 is also known as ATG18, ATG18A, WIPI49.