GABARAPL2

GABARAPL2 (GABA Type A Receptor Associated Protein Like 2) is a Protein Coding gene. Diseases associated with GABARAPL2 include neuronal ceroid lipofuscinosis and amyotrophic lateral sclerosis type 14. Among its related pathways are Cellular Senescence and Circadian entrainment. GO annotations related to this gene include microtubule binding and SNARE binding. An important paralog of this gene is MAP1LC3C.

Full Name

GABA type A receptor associated protein like 2

Function

Ubiquitin-like modifier involved in intra-Golgi traffic (By similarity).

Modulates intra-Golgi transport through coupling between NSF activity and SNAREs activation (By similarity).

It first stimulates the ATPase activity of NSF which in turn stimulates the association with GOSR1 (By similarity).

Involved in autophagy (PubMed:20418806, PubMed:23209295).

Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production (PubMed:20418806, PubMed:23209295).

Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (PubMed:20418806, PubMed:23209295).

Biological Process

Autophagosome assembly Source: GO_Central
Autophagy Source: UniProtKB
Autophagy of mitochondrion Source: GO_Central
Cellular response to nitrogen starvation Source: GO_Central
Intra-Golgi vesicle-mediated transport Source: UniProtKB
Macroautophagy Source: GO_Central
Negative regulation of proteasomal protein catabolic process Source: BHF-UCL
Positive regulation of ATPase activity Source: UniProtKB
Protein localization to endoplasmic reticulum Source: UniProtKB
Protein transport Source: UniProtKB-KW

Cellular Location

Endoplasmic reticulum membrane; Golgi apparatus; Autophagosome

PTM

The precursor molecule is cleaved by ATG4B to form the cytosolic form, GABARAPL2-I. This is activated by APG7L/ATG7, transferred to ATG3 and conjugated to phospholipid to form the membrane-bound form, GABARAPL2-II. ATG4B also mediates the delipidation required for GABARAPL1 recycling when autophagosomes fuse with lysosomes.