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Literature summary for 3.1.3.4 extracted from

  • Kok, B.P.; Skene-Arnold, T.D.; Ling, J.; Benesch, M.G.; Dewald, J.; Harris, T.E.; Holmes, C.F.; Brindley, D.N.
    Conserved residues in the N terminus of lipin-1 are required for binding to protein phosphatase-1c, nuclear translocation, and phosphatidate phosphatase activity (2014), J. Biol. Chem., 289, 10876-10886.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.3.4

Cloned(Commentary)

Cloned (Comment) Organism
expression in HEK-293 cell Homo sapiens

Protein Variants

Protein Variants Comment Organism
D712E/D714E catalytically inactive. Mutant binds to serine/threonine protein phosphatase-1 catalytic subunit to the same extent as wild-type Homo sapiens
F87A mutant based on non-phosphorylatable mutant, in which 21 serine/threonine residues are mutated to alanine. The additional mutation leads to n intermediate phenotype in binding to serine/threonine protein phosphatase-1 catalytic subunit Homo sapiens
I67A/I69A mutant based on non-phosphorylatable mutant, in which 21 serine/threonine residues are mutated to alanine. The additional mutation leads to a decrase in binding to serine/threonine protein phosphatase-1 catalytic subunit Homo sapiens
L58A mutant based on non-phosphorylatable mutant, in which 21 serine/threonine residues are mutated to alanine. The additional mutation does not affect binding to serine/threonine protein phosphatase-1 catalytic subunit Homo sapiens
L80A mutant based on non-phosphorylatable mutant, in which 21 serine/threonine residues are mutated to alanine. The additional mutation leads to n intermediate phenotype in binding to serine/threonine protein phosphatase-1 catalytic subunit Homo sapiens
additional information mutation of the HVRF binding motif to HARA causes a decrease in binding to serine/threonine protein phosphatase-1 catalytic subunit, blocks nuclear localization and phosphatidate phosphatase activity Homo sapiens
V57A mutant based on non-phosphorylatable mutant, in which 21 serine/threonine residues are mutated to alanine. The additional mutation does not affect binding to serine/threonine protein phosphatase-1 catalytic subunit Homo sapiens
V64A mutant based on non-phosphorylatable mutant, in which 21 serine/threonine residues are mutated to alanine. The additional mutation does not affect binding to serine/threonine protein phosphatase-1 catalytic subunit Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ may partly substitute for Mg2+ in binding to to serine/threonine protein phosphatase-1 catalytic subunit Homo sapiens
Mg2+ lipin-1 binding to to serine/threonine protein phosphatase-1 catalytic subunit depends on presence of Mg2+ Homo sapiens
Mn2+ may substitute for Mg2+ in binding to to serine/threonine protein phosphatase-1 catalytic subunit Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q14693
-
-

Synonyms

Synonyms Comment Organism
lipin-1
-
 Homo sapiens

General Information

General Information Comment Organism
metabolism isoform lipin-1 binds to serine/threonine protein phosphatase-1 catalytic subunit through a HVRF binding motif. Mutating the HVRF motif in the highly conserved N terminus of lipin-1 greatly decreases serine/threonine protein phosphatase-1 catalytic subunit interaction. Mutations of other residues in the N terminus of lipin-1 also modulate serine/threonine protein phosphatase-1 catalytic subunit binding. Serine/threonine protein phosphatase-1 catalytic subuni binds poorly to a phosphomimetic mutant of lipin-1 andbinds well to the non-phosphorylatable lipin-1 mutant. Mutating the HVRFmotif also abrogates the nuclear translocation and phosphatidate phosphatase activity of lipin-1 Homo sapiens