LYPLA1
LYPLA1 (lysophospholipase 1, also known as acyl-protein thioesterase 1, APT1, APT-1 and LPL1) is an AB hydrolase that removes palmitate from S-acylated proteins. It also has lysophospholipase activity, although its thioesterase activity is much higher. Browse Assay Genie's current range of LYPLA1 research reagents below, or read on for the biology behind the target.
LYPLA1 acts as an acyl-protein thioesterase. It hydrolyses fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins and HRAS. As a palmitoyl thioesterase it catalyses the depalmitoylation of substrates including ADRB2, KCNMA1 and SQSTM1. The NCBI Gene summary notes that the protein may be involved in Ras localisation and signalling.
The enzyme also works as a lysophospholipase. It hydrolyses lysophosphatidylcholine (lyso-PC), and also lysophosphatidylethanolamine, lysophosphatidylinositol and lysophosphatidylserine. Its thioesterase activity is much higher than its lysophospholipase activity. During blood coagulation, LYPLA1 contributes to the production of lysophosphatidic acid (LPA). It cleaves plasma phospholipids to generate lysophospholipids, which ENPP2 then uses as substrates to make LPA.
LYPLA1 is a negative regulator of autophagy. By acting on SQSTM1, it affects the palmitoylation of this protein, which decreases the affinity between SQSTM1 and ATG8 proteins. This in turn reduces the recruitment of ubiquitinated cargo proteins to autophagosomes. The LYPLA1 protein belongs to the AB hydrolase superfamily (AB hydrolase 2 family) and functions as a homodimer. It is found in the cytoplasm, cell membrane, nuclear membrane and endoplasmic reticulum. HGNC places the LYPLA1 gene in the depalmitoylase and thioester hydrolase groups, and its previous name was lysophospholipase I. Alternate splicing produces multiple transcript variants, and pseudogenes exist on chromosomes 4, 6 and 7.
LYPLA1 reverses S-palmitoylation of cysteine residues, making it a key enzyme for studying dynamic depalmitoylation of proteins such as G alpha subunits and HRAS.
The enzyme may be involved in Ras localisation and signalling through its action on palmitoylated HRAS.
LYPLA1 negatively regulates autophagy by controlling SQSTM1 palmitoylation, which affects SQSTM1 binding to ATG8 proteins and cargo recruitment.
LYPLA1 hydrolyses several lysophospholipids and contributes to LPA production during blood coagulation, linking it to lipid signalling.
LYPLA1 is an acyl-protein thioesterase that removes palmitate from S-acylated cysteines in proteins such as trimeric G alpha proteins, HRAS, ADRB2, KCNMA1 and SQSTM1. It also hydrolyses lysophospholipids, though its thioesterase activity is much higher than its lysophospholipase activity.
LYPLA1 is also called acyl-protein thioesterase 1, APT1, APT-1 and LPL1. Its previous HGNC name was lysophospholipase I. Alternate splicing of the LYPLA1 gene gives multiple transcript variants, and pseudogenes have been defined on chromosomes 4, 6 and 7.
Yes. The mouse and rat orthologs are both named Lypla1. The human protein belongs to the AB hydrolase superfamily (AB hydrolase 2 family) and functions as a homodimer. Check the datasheet of any product for its validated reactivity.
Depalmitoylases, substrates, autophagy regulators and lysophospholipid pathway proteins related to LYPLA1.
Gene and protein annotations from HGNC, NCBI Gene and UniProt O75608; product specifications from Assay Genie datasheets.