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Literature summary for 2.3.1.15 extracted from

  • Bratschi, M.W.; Burrowes, D.P.; Kulaga, A.; Cheung, J.F.; Alvarez, A.L.; Kearley, J.; Zaremberg, V.
    Glycerol-3-phosphate acyltransferases gat1p and gat2p are microsomal phosphoproteins with differential contributions to polarized cell growth (2009), Eukaryot. Cell, 8, 1184-1196.
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome subcellular localization of Gat1p and Gat2p are compared using fluorescence microscopy and subcellular fractionation using equilibrium density gradients. Gat1p and Gat2p overlap mostly in their localization and are microsomal GPATs, localized to both perinuclear and cortical endoplasmic reticula in actively proliferating cells Saccharomyces cerevisiae
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Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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possesses two GPAT
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Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein
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Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
GAT1p
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Saccharomyces cerevisiae
GAT2p
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Saccharomyces cerevisiae
glycerol-3-phosphate acyltransferase 1
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Saccharomyces cerevisiae
GPAT
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Saccharomyces cerevisiae

General Information

General Information Comment Organism
malfunction loss of function of Gat1p and Gat2p is masked by the compensatory effect of their redundant partner. The complete lack of GPAT results in cell death, with multibudded cells containing divided nuclei Saccharomyces cerevisiae
physiological function overexpression Gat1p in the absence of endogenous GPATs results in elongated cells with a normal cortical edoplasmic reticulum positioned underneath the plasma membrane, while excess Gat2p results in larger and round cells with an irregular layout of membranes, with pronounced invaginations also affecting the plasma membrane morphology Saccharomyces cerevisiae