Cloned (Comment) | Organism |
---|---|
V5-tagged lipin-1alpha, lipin-1beta, lipin-2 and lipin-3 expression vectors. HEK-293A cells transfected with plasmids expressing V5-tagged proteins. HeLa cells transfected with expression plasmids for V5-lipin-1beta and CFP-SUMO-1 or their mutants. SH-SY5Y cells stably expressing pcDNA3, lipin-1alpha-V5 or lipin-1alpha-K566R/K596R-V5. Cerebrocortical neurons from embryonic day 17 rat embryos transfected either with V5-tagged lipin-1alpha or lipin-1beta, or with the corresponding double sumoylation site mutants | Mus musculus |
Protein Variants | Comment | Organism |
---|---|---|
D679E | mutation in lipin-1alpha, does not lead to a diminished sumoylation | Mus musculus |
G84R | mutation in lipin-1alpha, does not lead to a diminished sumoylation | Mus musculus |
K566R/K596R | blocks lipin-1alpha sumoylation. In embryonic cortical neurons or SH-SY5Y clones, almost completely loses its nuclear localization compared to wild-type, although its cytoplasmic localization remains unchanged. Retains Mg2+-dependent phosphatase activity for phosphatidic acid (C8), but not for lysophosphatidic acid (C18:1) | Mus musculus |
K599R/K626R | lipin-1beta mutant, is not modified by SUMO-1 in an in vitro sumoylation reaction | Mus musculus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
additional information | in embryonic cortical neurons, lipin-1beta shows exclusively cytoplasmic localization. In SH-SY5Y clones, ectopic lipin-1a exhibits both nuclear and cytosolic localization, with a higher concentration in the nucleus, whereas lipin-1alpha is concentrated in the cytoplasm in HEK-93A cells. Sumoylation facilitates the nuclear localization and transcriptional coactivator behavior of lipin-1alpha in embryonic cortical neurons | Mus musculus | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | assay buffer | Mus musculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
V5-tagged proteins immunopurified | Mus musculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
brain | lipin-1, whereas lipin-1alpha is the predominant form | Mus musculus | - |
liver | lipin-1 | Mus musculus | - |
muscle | highest level of lipin-1 | Mus musculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
lysophosphatidic acid + H2O | - |
Mus musculus | monoacylglycerol + phosphate | - |
? | |
phosphatidic acid + H2O | - |
Mus musculus | 1,2-diacyl-sn-glycerol + phosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
lipin-1 | - |
Mus musculus |
lipin-2 | - |
Mus musculus |
lipin-3 | - |
Mus musculus |
LPP3 | - |
Mus musculus |
PAP | - |
Mus musculus |
phosphatidic acid phosphohydrolase | - |
Mus musculus |
General Information | Comment | Organism |
---|---|---|
malfunction | nuclear localization is abrogated by mutating the consensus sumyolation motifs. Sumoylation site mutant of lipin-1alpha loses the capacity to coactivate the transcriptional (co-) activators PGC-1alpha and MEF2, consistent with its nuclear exclusion | Mus musculus |
physiological function | lipin-1alpha may act as a sumoylation-regulated transcriptional coactivator in brain. Sumoylated forms of lipin-1 in muscle and liver are only marginally present. Lipin-1 (including both the alpha and beta isoforms) is modified by sumoylation at two consensus sumoylation sites, is sumoylated at relatively high levels in brain. No sumoylation of the related proteins lipin-2 and lipin-3 | Mus musculus |