BIOMAT Database Logo BIOMAT Database Logo

Mutations at position 1122 in the catalytic domain of the mouse ras-specific guanine nucleotide exchange factor CDC25Mm originate both loss-of-function and gain-of-function proteins. 1998

V Carrera, and A Moroni, and E Martegani, and C Volponi, and R H Cool, and L Alberghina, and M Vanoni
Dipartimento di Fisiologia e Biochimica Generali Sezione di Biochímica Comparata, Università degli Studi di Milano, Milan, Italy.

The role of two residues within the catalytic domain of CDC25Mm, a mouse ras-specific guanine nucleotide exchange factor (GEF), was investigated by site-directed mutagenesis. The function of the mutant proteins was tested in vivo in both a Saccharomyces cerevisiae cdc25 complementation assay and in a mammalian fos-luciferase assay, and in in vitro assays on human and yeast Ras proteins. Mutants CDC25Mm(E1048K) and CDC25Mm(S1122V) were shown to be (partly) inactive proteins, similar to their yeast homologs. Mutant CDC25Mm(S1122A) showed higher nucleotide exchange activity than the wild type protein on the basis of both in vitro and in vivo assays. Thus, alanine and valine substitutions at position 1122 within the GEF catalytic domain originate mutations with opposite biological properties, indicating an important role for position 1122 in GEF function.

UI MeSH Term Description Entries
D010749 Phosphoprotein Phosphatases A group of enzymes removing the SERINE- or THREONINE-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (Enzyme Nomenclature, 1992) Phosphoprotein Phosphatase,Phosphoprotein Phosphohydrolase,Protein Phosphatase,Protein Phosphatases,Casein Phosphatase,Ecto-Phosphoprotein Phosphatase,Nuclear Protein Phosphatase,Phosphohistone Phosphatase,Phosphoprotein Phosphatase-2C,Phosphoseryl-Protein Phosphatase,Protein Phosphatase C,Protein Phosphatase C-I,Protein Phosphatase C-II,Protein Phosphatase H-II,Protein-Serine-Threonine Phosphatase,Protein-Threonine Phosphatase,Serine-Threonine Phosphatase,Threonine Phosphatase,Ecto Phosphoprotein Phosphatase,Phosphatase C, Protein,Phosphatase C-I, Protein,Phosphatase C-II, Protein,Phosphatase H-II, Protein,Phosphatase, Casein,Phosphatase, Ecto-Phosphoprotein,Phosphatase, Nuclear Protein,Phosphatase, Phosphohistone,Phosphatase, Phosphoprotein,Phosphatase, Phosphoseryl-Protein,Phosphatase, Protein,Phosphatase, Protein-Serine-Threonine,Phosphatase, Protein-Threonine,Phosphatase, Serine-Threonine,Phosphatase, Threonine,Phosphatase-2C, Phosphoprotein,Phosphatases, Phosphoprotein,Phosphatases, Protein,Phosphohydrolase, Phosphoprotein,Phosphoprotein Phosphatase 2C,Phosphoseryl Protein Phosphatase,Protein Phosphatase C I,Protein Phosphatase C II,Protein Phosphatase H II,Protein Phosphatase, Nuclear,Protein Serine Threonine Phosphatase,Protein Threonine Phosphatase,Serine Threonine Phosphatase
D006150 Guanine Nucleotides Guanine Nucleotide,Guanosine Phosphates,Nucleotide, Guanine,Nucleotides, Guanine,Phosphates, Guanosine
D006224 Cricetinae A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS. Cricetus,Hamsters,Hamster
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D012441 Saccharomyces cerevisiae A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement. Baker's Yeast,Brewer's Yeast,Candida robusta,S. cerevisiae,Saccharomyces capensis,Saccharomyces italicus,Saccharomyces oviformis,Saccharomyces uvarum var. melibiosus,Yeast, Baker's,Yeast, Brewer's,Baker Yeast,S cerevisiae,Baker's Yeasts,Yeast, Baker
D014162 Transfection The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES. Transfections
D016297 Mutagenesis, Site-Directed Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion. Mutagenesis, Oligonucleotide-Directed,Mutagenesis, Site-Specific,Oligonucleotide-Directed Mutagenesis,Site-Directed Mutagenesis,Site-Specific Mutagenesis,Mutageneses, Oligonucleotide-Directed,Mutageneses, Site-Directed,Mutageneses, Site-Specific,Mutagenesis, Oligonucleotide Directed,Mutagenesis, Site Directed,Mutagenesis, Site Specific,Oligonucleotide Directed Mutagenesis,Oligonucleotide-Directed Mutageneses,Site Directed Mutagenesis,Site Specific Mutagenesis,Site-Directed Mutageneses,Site-Specific Mutageneses
D016466 CHO Cells CELL LINE derived from the ovary of the Chinese hamster, Cricetulus griseus (CRICETULUS). The species is a favorite for cytogenetic studies because of its small chromosome number. The cell line has provided model systems for the study of genetic alterations in cultured mammalian cells. CHO Cell,Cell, CHO,Cells, CHO
D016475 3T3 Cells Cell lines whose original growing procedure consisted being transferred (T) every 3 days and plated at 300,000 cells per plate (J Cell Biol 17:299-313, 1963). Lines have been developed using several different strains of mice. Tissues are usually fibroblasts derived from mouse embryos but other types and sources have been developed as well. The 3T3 lines are valuable in vitro host systems for oncogenic virus transformation studies, since 3T3 cells possess a high sensitivity to CONTACT INHIBITION. 3T3 Cell,Cell, 3T3,Cells, 3T3
D016762 Genes, fos Retrovirus-associated DNA sequences (fos) originally isolated from the Finkel-Biskis-Jinkins (FBJ-MSV) and Finkel-Biskis-Reilly (FBR-MSV) murine sarcoma viruses. The proto-oncogene protein c-fos codes for a nuclear protein which is involved in growth-related transcriptional control. The insertion of c-fos into FBJ-MSV or FBR-MSV induces osteogenic sarcomas in mice. The human c-fos gene is located at 14q21-31 on the long arm of chromosome 14. c-fos Genes,fos Genes,v-fos Genes,c-fos Proto-Oncogenes,v-fos Oncogenes,c fos Genes,c fos Proto Oncogenes,c-fos Gene,c-fos Proto-Oncogene,fos Gene,v fos Genes,v fos Oncogenes,v-fos Gene,v-fos Oncogene

Related Publications

V Carrera, and A Moroni, and E Martegani, and C Volponi, and R H Cool, and L Alberghina, and M Vanoni
The Ras Guanine nucleotide Exchange Factor CDC25Mm is present at the synaptic junction.
August 1997, Experimental cell research,
V Carrera, and A Moroni, and E Martegani, and C Volponi, and R H Cool, and L Alberghina, and M Vanoni
The isolated catalytic hairpin of the Ras-specific guanine nucleotide exchange factor Cdc25Mm retains nucleotide dissociation activity but has impaired nucleotide exchange activity.
December 2005, FEBS letters,
V Carrera, and A Moroni, and E Martegani, and C Volponi, and R H Cool, and L Alberghina, and M Vanoni
Kinetic analysis by fluorescence of the interaction between Ras and the catalytic domain of the guanine nucleotide exchange factor Cdc25Mm.
May 1998, Biochemistry,
V Carrera, and A Moroni, and E Martegani, and C Volponi, and R H Cool, and L Alberghina, and M Vanoni
Analysis of the secondary structure of the catalytic domain of mouse Ras exchange factor CDC25Mm.
April 1998, Biochimica et biophysica acta,
V Carrera, and A Moroni, and E Martegani, and C Volponi, and R H Cool, and L Alberghina, and M Vanoni
The minimal active domain of the mouse ras exchange factor CDC25Mm.
January 1995, Biochemical and biophysical research communications,
V Carrera, and A Moroni, and E Martegani, and C Volponi, and R H Cool, and L Alberghina, and M Vanoni
Genetic mapping of the mouse CDC25Mm gene, a ras-specific guanine nucleotide-releasing factor, to chromosome 9.
May 1994, Genomics,
V Carrera, and A Moroni, and E Martegani, and C Volponi, and R H Cool, and L Alberghina, and M Vanoni
Sites of phosphorylation by protein kinase A in CDC25Mm/GRF1, a guanine nucleotide exchange factor for Ras.
January 2001, The Journal of biological chemistry,
V Carrera, and A Moroni, and E Martegani, and C Volponi, and R H Cool, and L Alberghina, and M Vanoni
Structure determination of the Ras-binding domain of the Ral-specific guanine nucleotide exchange factor Rlf.
September 1998, Biochemistry,
V Carrera, and A Moroni, and E Martegani, and C Volponi, and R H Cool, and L Alberghina, and M Vanoni
A dominant negative RAS-specific guanine nucleotide exchange factor reverses neoplastic phenotype in K-ras transformed mouse fibroblasts.
April 2000, Oncogene,
V Carrera, and A Moroni, and E Martegani, and C Volponi, and R H Cool, and L Alberghina, and M Vanoni
The guanine nucleotide exchange factor Ric-8A induces domain separation and Ras domain plasticity in Gαi1.
February 2015, Proceedings of the National Academy of Sciences of the United States of America,
Copied contents to your clipboard!