ArticleMolecular and cellular biology1996
The LIM domain-containing Dbm1 GTPase-activating protein is required for normal cellular morphogenesis in Saccharomyces cerevisiae.
Article in Molecular and cellular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 37 citations in OpenAlex.
- Regulation of Cdc42 for polarized growth in budding yeast.Microbial cell (Graz, Austria) · 2020Review
- Fine-tuning the orientation of the polarity axis by Rga1, a Cdc42 GTPase-activating protein.Molecular biology of the cell · 2017Article
- Evolutionary dynamics in the fungal polarization network, a mechanistic perspective.Biophysical reviews · 2017Review
- Calcineurin, the CaMolecular biology of the cell · 2017Article
- Regulation of Cdc42 polarization by the Rsr1 GTPase and Rga1, a Cdc42 GTPase-activating protein, in budding yeast.Journal of cell science · 2015Article
- The GTPase-activating protein Rga1 interacts with Rho3 GTPase and may regulate its function in polarized growth in budding yeast.PloS one · 2015Article
- Polarization of Diploid Daughter Cells Directed by Spatial Cues and GTP Hydrolysis of Cdc42 in Budding YeastPloS one · 2013Article
- Cell polarization and cytokinesis in budding yeast.Genetics · 2012Review
- Morphogenesis and the cell cycle.Genetics · 2012Review
- Adjacent positioning of cellular structures enabled by a Cdc42 GTPase-activating protein-mediated zone of inhibition.The Journal of cell biology · 2007Article
- Regulation of cell diameter, For3p localization, and cell symmetry by fission yeast Rho-GAP Rga4p.Molecular biology of the cell · 2007Article
- Central roles of small GTPases in the development of cell polarity in yeast and beyond.Microbiology and molecular biology reviews : MMBR · 2007Review
- Pxl1p, a paxillin-like protein in Saccharomyces cerevisiae, may coordinate Cdc42p and Rho1p functions during polarized growth.Molecular biology of the cell · 2004Article
- The PXL1 gene of Saccharomyces cerevisiae encodes a paxillin-like protein functioning in polarized cell growth.Molecular biology of the cell · 2004Article
- The Rho-GAP Bem2p plays a GAP-independent role in the morphogenesis checkpoint.The EMBO journal · 2002Article
- GTPase-activating proteins for Cdc42.Eukaryotic cell · 2002Article
- Different domains of the essential GTPase Cdc42p required for growth and development of Saccharomyces cerevisiae.Molecular and cellular biology · 2001Article
- Identification of novel, evolutionarily conserved Cdc42p-interacting proteins and of redundant pathways linking Cdc24p and Cdc42p to actin polarization in yeast.Molecular biology of the cell · 2000Article
- Cdc42: An essential Rho-type GTPase controlling eukaryotic cell polarity.Microbiology and molecular biology reviews : MMBR · 1999Review
- The Cdc42 GTPase-associated proteins Gic1 and Gic2 are required for polarized cell growth in Saccharomyces cerevisiae.Genes & development · 1997Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Normal cell growth in the yeast Saccharomyces cerevisiae involves the selection of genetically determined bud sites where most growth is localized. Previous studies have shown that BEM2, which encodes a GTPase-activating protein (GAP) that is specific for the Rho-type GTPase Rho1p in vitro, is required for proper bud site selection and bud emergence. We show here that DBM1, which encodes another putative Rho-type GAP with two tandemly arranged cysteine-rich LIM domains, also is needed for proper bud site selection, as haploid cells lacking Dbm1p bud predominantly in a bipolar, rather than the normal axial, manner. Furthermore, yeast cells lacking both Bem2p and Dbm1p are inviable. The nonaxial budding defect of dbm1 mutants can be rescued partially by overproduction of Bem3p and is exacerbated by its absence. Since Bem3p has previously been shown to function as a GAP for Cdc42p, and also less efficiently for Rho1p, our results suggest that Dbm1p, like Bem2p and Bem3p, may function in vivo as a GAP for Cdc42p and/or Rho1p. Both LIM domains of Dbm1p are essential for its normal function. Point mutations that alter single conserved cysteine residues within either LIM domain result in mutant forms of Dbm1p that can no longer function in bud site selection but instead are capable of rescuing the inviability of bem2 mutants at 35 degrees C.
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