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Gene Review

CDC50  -  aminophospholipid translocase regulatory...

Saccharomyces cerevisiae S288c

Synonyms: Cell division control protein 50, YCR094W, YCR94W
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High impact information on CDC50

  • In addition, Rcy1p coimmunoprecipitated with Cdc50p-Drs2p [1].
  • Thus, LdMT and LdRos3 seem to form part of the same translocation machinery that determines flippase activity and miltefosine sensitivity in Leishmania, further supporting the consideration of CDC50/Lem3 proteins as beta subunits required for the normal functioning of P4-ATPases [2].
  • Cdc50p, a membrane protein in the endosomal/trans-Golgi network compartments, is a noncatalytic subunit of Drs2p, which is implicated in translocation of phospholipids across lipid bilayers [3].
  • Cdc50p, a transmembrane protein localized to the late endosome, is required for polarized cell growth in yeast [4].
  • Both Cdc50p and Drs2p were localized to the trans-Golgi network and late endosome [4].

Biological context of CDC50

  • Thus, phospholipid asymmetry plays an important role in the establishment of cell polarity; the Cdc50p/Lem3p family likely constitute potential subunits specific to unique P-type ATPases of the APT subfamily [4].
  • The disruption of the CDC50 gene revealed that it is not essential for growth, but the disruptant caused the same cold-sensitive phenotype as cdc50-1, suggesting that the cdc50-1 is a null mutation resulted from the mutation in the first codon [5].
  • We have cloned a gene that complements the cold-sensitive growth of cdc50-1 mutant strain of Saccharomyces cerevisiae at 14 degrees C. The CDC50 gene was found to be identical to YCR094w on chromosome III and contains 1173 nucleotides encoding 391 amino acids [5].
  • The cdc50 null mutant showed cold-sensitive cell cycle arrest with a small bud as reported previously [6].
  • The cdc50 mutant showed defects in a late stage of endocytosis but not in the internalization step [6].

Anatomical context of CDC50

  • Here, we show that SWA4 is allelic to CDC50, encoding a membrane protein previously shown to chaperone Drs2p from the endoplasmic reticulum to the Golgi complex [7].
  • As predicted by its amino acid sequence, Cdc50p appears to be a transmembrane protein because it was solubilized from the membranes by detergent treatment [6].
  • Most of the examined transport pathways in the Cdc50p-depleted gcs1Delta mutant were nearly normal, including endocytic transport to vacuoles, carboxypeptidase Y sorting, and the processing and secretion of invertase [8].

Associations of CDC50 with chemical compounds

  • Membrane topology and extracellular loop containing three Cys residues and one Asn-linked glycosylation site were evolutionarily conserved among mammalian CDC50 homologs and yeast Cdc50p homologs [9].

Physical interactions of CDC50

  • Cdc50p was coimmunoprecipitated with Drs2p from membrane protein extracts [4].

Other interactions of CDC50

  • Genetic studies suggest that CDC50 performs a function similar to DRS2, which encodes a P-type ATPase of the aminophospholipid translocase (APT) subfamily [4].
  • We identified CDC50 as a multicopy suppressor of the myo3 myo5-360 temperature-sensitive mutant, which is defective in organization of cortical actin patches [6].
  • We also found that the CDC39 gene was a multicopy suppressor of cdc50-1 mutation, suggesting that the CDC50 family is involved in regulation of transcription via CDC39 [5].
  • Three ORFs show limited homology with known proteins: NO330 with the recessive suppressor of secretory defect SAC1, NO325 with YCR094W identified during chromosome III sequencing; whereas NO315 presents a motif conserved in the dnaJ family [10].
  • These results suggest that Cdc50p-Drs2p plays an important role in the Arf1p-mediated formation of CCVs for the retrieval pathway from early endosomes to the TGN [8].


  1. Endocytic recycling in yeast is regulated by putative phospholipid translocases and the ypt31p/32p-rcy1p pathway. Furuta, N., Fujimura-Kamada, K., Saito, K., Yamamoto, T., Tanaka, K. Mol. Biol. Cell (2007) [Pubmed]
  2. Phospholipid translocation and miltefosine potency require both L. donovani miltefosine transporter and the new protein LdRos3 in Leishmania parasites. Pérez-Victoria, F.J., Sánchez-Cañete, M.P., Castanys, S., Gamarro, F. J. Biol. Chem. (2006) [Pubmed]
  3. Defects in structural integrity of ergosterol and the Cdc50p-Drs2p putative phospholipid translocase cause accumulation of endocytic membranes, onto which actin patches are assembled in yeast. Kishimoto, T., Yamamoto, T., Tanaka, K. Mol. Biol. Cell (2005) [Pubmed]
  4. Cdc50p, a protein required for polarized growth, associates with the Drs2p P-type ATPase implicated in phospholipid translocation in Saccharomyces cerevisiae. Saito, K., Fujimura-Kamada, K., Furuta, N., Kato, U., Umeda, M., Tanaka, K. Mol. Biol. Cell (2004) [Pubmed]
  5. The cloning and characterization of the CDC50 gene family in Saccharomyces cerevisiae. Radji, M., Kim, J.M., Togan, T., Yoshikawa, H., Shirahige, K. Yeast (2001) [Pubmed]
  6. Cdc50p, a conserved endosomal membrane protein, controls polarized growth in Saccharomyces cerevisiae. Misu, K., Fujimura-Kamada, K., Ueda, T., Nakano, A., Katoh, H., Tanaka, K. Mol. Biol. Cell (2003) [Pubmed]
  7. Roles for the drs2p-cdc50p complex in protein transport and phosphatidylserine asymmetry of the yeast plasma membrane. Chen, S., Wang, J., Muthusamy, B.P., Liu, K., Zare, S., Andersen, R.J., Graham, T.R. Traffic (2006) [Pubmed]
  8. The functional relationship between the Cdc50p-Drs2p putative aminophospholipid translocase and the Arf GAP Gcs1p in vesicle formation in the retrieval pathway from yeast early endosomes to the TGN. Sakane, H., Yamamoto, T., Tanaka, K. Cell Struct. Funct. (2006) [Pubmed]
  9. Identification and characterization of CDC50A, CDC50B and CDC50C genes in silico. Katoh, Y., Katoh, M. Oncol. Rep. (2004) [Pubmed]
  10. Sequencing analysis of a 15.4 kb fragment of yeast chromosome XIV identifies the RPD3, PAS8 and KRE1 loci, five new open reading frames. Maftahi, M., Nicaud, J.M., Levesque, H., Gaillardin, C. Yeast (1995) [Pubmed]
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