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Literature summary for 3.1.3.B4 extracted from

  • Lorente-Rodriguez, A.; Barlowe, C.
    Requirement for Golgi-localized PI(4)P in fusion of COPII vesicles with Golgi compartments (2011), Mol. Biol. Cell, 22, 216-229.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.3.B4

Application

Application Comment Organism
additional information usage of the recombinant Sac1p Sac1 phosphatase activity to deplete phosphatidylinositol-4-phosphate from semi-intact cell membranes, method development and optimization, overview Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
C392S catalytically inactive mutant Saccharomyces cerevisiae
additional information usage of the recombinant Sac1p Sac1 phosphatase activity to deplete phosphatidylinositol-4-phosphate from semi-intact cell membranes, method development and optimization, overview Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
N-ethylmaleimide NEM inactivation of Sac1 wild-type completely prevents its inhibitory activity in two-stage fusion reactions compared to mock treated Sac1 wild-type Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
 Saccharomyces cerevisiae 5783
-
microsome
-
 Saccharomyces cerevisiae
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Saccharomyces cerevisiae Sac1, a phosphoinositide lipid phosphatase, removes the phosphate residue from the inositol head group of phosphatidylinositol-4-phosphate ?
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information Sac1, a phosphoinositide lipid phosphatase, removes the phosphate residue from the inositol head group of phosphatidylinositol-4-phosphate Saccharomyces cerevisiae ?
-
 ?

Synonyms

Synonyms Comment Organism
phosphoinositide lipid phosphatase
-
 Saccharomyces cerevisiae
phosphoinositide phosphatase
-
 Saccharomyces cerevisiae
Sac1p
-
 Saccharomyces cerevisiae
Sac1p-phosphatase
-
 Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function mutant Sac1 C392S is a potent inhibitor of fusion of coat protein complex II, COPII, vesicles with Golgi compartments whereas the Sac1 WT protein does not display an equal inhibitory effect. The inhibitory effects of Sac1 wild-type are likely due to catalytic activity of the enzyme and not due to lipid ligand binding. Pretreatment of acceptor membranes with 50 microM Sac1 wild-type also causes an accumulation of diffusible vesicles in budding reactions and strong inhibition of SNARE complex formation Saccharomyces cerevisiae