GABARAPL1

GABARAPL1 (GABA Type A Receptor Associated Protein Like 1) is a Protein Coding gene. Diseases associated with GABARAPL1 include Alzheimer Disease 13 and Danon Disease. Among its related pathways are Autophagy - animal and Human cytomegalovirus infection. Gene Ontology (GO) annotations related to this gene include microtubule binding and GABA receptor binding. An important paralog of this gene is GABARAP.

Full Name

GABA Type A Receptor Associated Protein Like 1

Function

Ubiquitin-like modifier that increases cell-surface expression of kappa-type opioid receptor through facilitating anterograde intracellular trafficking of the receptor (PubMed:16431922).

Involved in formation of autophagosomal vacuoles (PubMed:20404487).

While LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (PubMed:20404487).

Through its interaction with the reticulophagy receptor TEX264, participates in the remodeling of subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover (PubMed:31006538, PubMed:31006537).

Biological Process

Autophagosome assembly Source: GO_Central
Autophagy of mitochondrion Source: GO_Central
Cellular response to nitrogen starvation Source: GO_Central
Macroautophagy Source: GO_Central

Cellular Location

Cytoskeleton; Golgi apparatus; Endoplasmic reticulum; Autophagosome; Cytoplasmic vesicle membrane

PTM

The precursor molecule is cleaved by ATG4B to form the cytosolic form, GABARAPL1-I (PubMed:20404487). This is activated by APG7L/ATG7, transferred to ATG3 and conjugated to phospholipid to form the membrane-bound form, GABARAPL1-II (PubMed:20404487). ATG4B also mediates the delipidation required for GABARAPL1 recycling when autophagosomes fuse with lysosomes (PubMed:20404487).
(Microbial infection) The Legionella effector RavZ is a deconjugating enzyme that produces an ATG8 product that would be resistant to reconjugation by the host machinery due to the cleavage of the reactive C-terminal glycine.