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Literature summary for 3.1.3.4 extracted from

  • Liu, G.H.; Gerace, L.
    Sumoylation regulates nuclear localization of lipin-1alpha in neuronal cells (2009), PLoS ONE, 4, e7031.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.3.4

Cloned(Commentary)

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

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

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
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Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ assay buffer Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
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-
-

Purification (Commentary)

Purification (Comment) Organism
V5-tagged proteins immunopurified Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
brain lipin-1, whereas lipin-1alpha is the predominant form Mus musculus
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liver lipin-1 Mus musculus
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muscle highest level of lipin-1 Mus musculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
lysophosphatidic acid + H2O
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 Mus musculus monoacylglycerol + phosphate
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 ?
phosphatidic acid + H2O
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 Mus musculus 1,2-diacyl-sn-glycerol + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
lipin-1
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 Mus musculus
lipin-2
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 Mus musculus
lipin-3
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 Mus musculus
LPP3
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 Mus musculus
PAP
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 Mus musculus
phosphatidic acid phosphohydrolase
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 Mus musculus

General Information

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