GCS1/YDL226C Literature Guide Help

Other names published for GCS1: YDL226C

GCS1 - Genetic Interactions (26)

ReferenceOther Genes Addressed
Benjamin JJ, et al.  (2011) Dysregulated Arl1, a regulator of post-Golgi vesicle tethering, can inhibit endosomal transport and cell proliferation in yeast. Mol Biol Cell 22(13):2337-47
Benjamin JJ, et al.  (2011) The Yeast Arf GTPase-activating Protein Age1 Is Regulated by Phospholipase D for Post-Golgi Vesicular Transport. J Biol Chem 286(7):5187-96
Lin L, et al.  (2011) The antibiotic gentamicin inhibits specific protein trafficking functions of the arf1/2 family of GTPases. Antimicrob Agents Chemother 55(1):246-54
Webster MT, et al.  (2010) Vesicle trafficking maintains nuclear shape in Saccharomyces cerevisiae during membrane proliferation. J Cell Biol 191(6):1079-88
Kim JH, et al.  (2009) The unfolded protein response is necessary but not sufficient to compensate for defects in disulfide isomerization. J Biol Chem 284(16):10400-8
Schindler C, et al.  (2009) The GAP domain and the SNARE, coatomer and cargo interaction region of the ArfGAP2/3 Glo3 are sufficient for Glo3 function. Traffic 10(9):1362-75
Aguilera-Romero A, et al.  (2008) The yeast p24 complex is required for the formation of COPI retrograde transport vesicles from the Golgi apparatus. J Cell Biol 180(4):713-20
Connolly JE and Engebrecht J  (2006) The Arf-GTPase-activating protein Gcs1p is essential for sporulation and regulates the phospholipase D Spo14p. Eukaryot Cell 5(1):112-24
Liu YW, et al.  (2006) Arl1p is involved in transport of the GPI-anchored protein Gas1p from the late Golgi to the plasma membrane. J Cell Sci 119(Pt 18):3845-55
Robinson M, et al.  (2006) The Gcs1 Arf-GAP mediates Snc1,2 v-SNARE retrieval to the Golgi in yeast. Mol Biol Cell 17(4):1845-58
Sakane H, et al.  (2006) 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. Cell Struct Funct 31(2):87-108
Song XF, et al.  (2006) RPA, a class II ARFGAP protein, activates ARF1 and U5 and plays a role in root hair development in Arabidopsis. Plant Physiol 141(3):966-76
Liu YW, et al.  (2005) Role for Gcs1p in regulation of Arl1p at trans-Golgi compartments. Mol Biol Cell 16(9):4024-33
Wong TA, et al.  (2005) Membrane metabolism mediated by Sec14 family members influences Arf GTPase activating protein activity for transport from the trans-Golgi. Proc Natl Acad Sci U S A 102(36):12777-82
Lewis SM, et al.  (2004) The ArfGAP Glo3 is required for the generation of COPI vesicles. Mol Biol Cell 15(9):4064-72
Zhang CJ, et al.  (2003) Four ARF GAPs in Saccharomyces cerevisiae have both overlapping and distinct functions. Yeast 20(4):315-30
Li X, et al.  (2002) Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex. J Cell Biol 157(1):63-77
Zhang CJ, et al.  (2002) Genetic interactions link ARF1, YPT31/32 and TRS130. Yeast 19(12):1075-86
Poon PP, et al.  (2001) The Gcs1 and Age2 ArfGAP proteins provide overlapping essential function for transport from the yeast trans-Golgi network. J Cell Biol 155(7):1239-50
Blader IJ, et al.  (1999) GCS1, an Arf guanosine triphosphatase-activating protein in Saccharomyces cerevisiae, is required for normal actin cytoskeletal organization in vivo and stimulates actin polymerization in vitro. Mol Biol Cell 10(3):581-96
Poon PP, et al.  (1999) Retrograde transport from the yeast Golgi is mediated by two ARF GAP proteins with overlapping function. EMBO J 18(3):555-64
Zhang CJ, et al.  (1998) A family of Arf effectors defined as suppressors of the loss of Arf function in the yeast Saccharomyces cerevisiae. J Biol Chem 273(31):19792-6
Poon PP, et al.  (1996) Saccharomyces cerevisiae Gcs1 is an ADP-ribosylation factor GTPase-activating protein. Proc Natl Acad Sci U S A 93(19):10074-7
Wang X, et al.  (1996) Prenylated isoforms of yeast casein kinase I, including the novel Yck3p, suppress the gcs1 blockage of cell proliferation from stationary phase. Mol Cell Biol 16(10):5375-85
Filipak M, et al.  (1992) Mitochondrial DNA loss by yeast reentry-mutant cells conditionally unable to proliferate from stationary phase. Curr Genet 22(6):471-7
Drebot MA, et al.  (1987) A yeast mutant conditionally defective only for reentry into the mitotic cell cycle from stationary phase. Proc Natl Acad Sci U S A 84(22):7948-52