MAP1LC3A

MAP1A and MAP1B are microtubule-associated proteins which mediate the physical interactions between microtubules and components of the cytoskeleton. MAP1A and MAP1B each consist of a heavy chain subunit and multiple light chain subunits. The protein encoded by this gene is one of the light chain subunits and can associate with either MAP1A or MAP1B. Two transcript variants encoding different isoforms have been found for this gene. The expression of variant 1 is suppressed in many tumor cell lines, suggesting that may be involved in carcinogenesis. [provided by RefSeq, Feb 2012]

Microtubule Associated Protein 1 Light Chain 3 Alpha

Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes) (PubMed:20713600, PubMed:24290141).
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:20713600).
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).

Autophagosome assemblyManual Assertion Based On ExperimentIMP:UniProtKB
Autophagosome maturationManual Assertion Based On ExperimentIDA:UniProtKB
Autophagy of mitochondrionManual Assertion Based On ExperimentIGI:MGI
Cellular response to amino acid starvationIEA:Ensembl
Cellular response to copper ionIEA:Ensembl
Cellular response to hydrogen peroxideIEA:Ensembl
Cellular response to nitrogen starvationManual Assertion Based On ExperimentIBA:GO_Central
Cellular response to starvationManual Assertion Based On ExperimentIDA:UniProtKB
MacroautophagyManual Assertion Based On ExperimentIDA:UniProtKB
Response to iron(II) ionIEA:Ensembl
Response to lead ionIEA:Ensembl
Response to morphineIEA:Ensembl

Cytoplasmic vesicle, autophagosome membrane
Endomembrane system
Cytoplasm, cytoskeleton
LC3-II binds to the autophagic membranes.

The precursor molecule is cleaved by ATG4 (ATG4A, ATG4B, ATG4C or ATG4D) to expose the glycine at the C-terminus and form the cytosolic form, LC3-I (PubMed:15187094, PubMed:30661429).
The processed form is then activated by APG7L/ATG7, transferred to ATG3 and conjugated to phosphatidylethanolamine (PE) phospholipid to form the membrane-bound form, LC3-II (PubMed:15187094).
During non-canonical autophagy, the processed form is conjugated to phosphatidylserine (PS) phospholipid (PubMed:33909989).
ATG4 proteins also mediate the delipidation of PE-conjugated forms (PubMed:32686895, PubMed:33909989).
In addition, ATG4B and ATG4D mediate delipidation of ATG8 proteins conjugated to PS during non-canonical autophagy (PubMed:33909989).
ATG4B constitutes the major protein for proteolytic activation (PubMed:30661429, PubMed:33909989).
ATG4D is the main enzyme for delipidation activity (By similarity).
(Microbial infection) The Legionella effector RavZ is a deconjugating enzyme that hydrolyzes the amide bond between the C-terminal glycine residue and an adjacent aromatic residue in ATG8 proteins conjugated to phosphatidylethanolamine (PE), producing an ATG8 protein that is resistant to reconjugation by the host machinery due to the cleavage of the reactive C-terminal glycine (PubMed:23112293, PubMed:32686895, PubMed:31722778).
RavZ is also able to mediate delipidation of ATG8 proteins conjugated to phosphatidylserine (PS) (PubMed:33909989).
Phosphorylation at Ser-12 by PKA inhibits conjugation to phosphatidylethanolamine (PE).