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Literature summary for 7.6.2.1 extracted from

  • Liu, K.; Hua, Z.; Nepute, J.A.; Graham, T.R.
    Yeast P4-ATPases Drs2p and Dnf1p are essential cargos of the NPFXD/Sla1p endocytic pathway (2007), Mol. Biol. Cell, 18, 487-500.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of GFP-tagged Drs2p and HA-tagged Drf1p wild-type and mutant enzymes in Saccharomyces cerevisiae, subcloning in Escherichia coli strains XL1-Blue and DH5alpha Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
additional information construction of yeast knockout strains lacking Drs2p and/or Drf1p activity, the pan1-20 temperature-sensitive mutant is constitutively defective for Ub-dependent endocytosis but is not defective for NPFXD-dependent endocytosis at the permissive growth temperature. To sustain viability of pan1-20, Drs2p must be endocytosed through the NPFXD/Sla1p pathway Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
Golgi apparatus Drs2p, which has multiple endocytosis signals, including two NPFXDs near the C terminus and PEST-like sequences near the N terminus that may mediate ubiquitin-dependent endocytosis, localizes to the trans-Golgi network in wild-type cells and accumulates on the plasma membrane when both the Ub- and NPFXD-dependent endocytic mechanisms are inactivated, the C-terminal and N-terminal NPFXD motifs ar functionally required by Drs2p and Drf1p, overview Saccharomyces cerevisiae 5794
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membrane
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Saccharomyces cerevisiae 16020
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additional information P4-ATPases Drs2p and Dnf1p cycle between the exocytic and endocytic pathways, and maintain a steady-state localization to internal organelles requiring endocytosis Saccharomyces cerevisiae
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plasma membrane internalization of Dnf1p from the plasma membrane uses an NPFXD endocytosis signal and its recognition by Sla1p, part of an endocytic coat/adaptor complex with clathrin, Pan1p, Sla2p/End4p, and End3p Saccharomyces cerevisiae 5886
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + phospholipid/in Saccharomyces cerevisiae P4-ATPases Drs2p and Dnf1p cycle between the exocytic and endocytic pathways, and maintain a steady-state localization to internal organelles requiring endocytosis signals, Drs2p is an essential endocytic cargo in cells compromised for Ub-dependent endocytosis ADP + phosphate + phospholipid/out
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?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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diverse strains, overview
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Purification (Commentary)

Purification (Comment) Organism
native enzymes partially by subcellular fractionation Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + phospholipid/in P4-ATPases Drs2p and Dnf1p cycle between the exocytic and endocytic pathways, and maintain a steady-state localization to internal organelles requiring endocytosis signals, Drs2p is an essential endocytic cargo in cells compromised for Ub-dependent endocytosis Saccharomyces cerevisiae ADP + phosphate + phospholipid/out
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?
ATP + H2O + phospholipid/in ATP-dependent transport of phospholipids from outer to the inner monolayer of the cell membrane to maintain lipid asymmetry, the C-terminal and N-terminal NPFXD motifs ar functionally required by Drs2p and Drf1p, respectively, overview Saccharomyces cerevisiae ADP + phosphate + phospholipid/out
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?

Subunits

Subunits Comment Organism
More the C-tail is essential for Drs2p function in protein transport bearing the functionally required NPFXD motifs, Drs2p and Drf1p both contain an N-terminally located NPFXD motif, located in the cytoplasmic tail in Drf1p, importnat for activity, overview Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
Dnf1p
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Saccharomyces cerevisiae
Drs2p
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Saccharomyces cerevisiae
flippase
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Saccharomyces cerevisiae
More the enzymes belong to the P4-ATPase family Saccharomyces cerevisiae
phospholipid translocase
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Saccharomyces cerevisiae