Sequence and expression of the discoidin I gene family in Dictyostelium discoideum

Poole, Stephen J.; Firtel, Richard A.; Lamar, E.; Röwekamp, Walter

doi:10.1016/0022-2836(81)90278-3

Cited by 172 publications

(97 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The function of the discoidins is unclear (reviewed in reference 3). This report demonstrates that mutant cells overproduced at least two electrophoretically distinguishable species of discoidin I, known to be the products of different structural genes (20,28). Two other proteins normally induced during early development were not affected.…”

mentioning

confidence: 72%

“…In developing methods to purify the 33K protein, it became apparent that its fractionation behavior and solubility properties, as well as its subunit size, resembled those of discoidin I. Discoidins I and II are carbohydrate-binding proteins produced by D. discoideum cells during development and axenic growth (see below). There are three isoelectric forms of discoidin I, and each form is the product of a different gene (20,28). To test the relationship between discoidin I and the 33K protein of MC2 cells, discoidins were purified from axenically grown AX3 cells by affinity chromatography on Sepharose (26); this preparation method yields both discoidins I and II.…”

mentioning

confidence: 99%

“…2a) [20]. However, its apparent molecular weight on SDS-gels ranges from 26K [9] to 33K [30], depending on the gel system and standards used.)…”

mentioning

confidence: 99%

See 2 more Smart Citations

Overproduction of discoidin I by a temperature-sensitive motility mutant of Dictyostelium discoideum.

Biswas¹,

Kayman²,

Clarke³

1984

Mol. Cell. Biol.

View full text Add to dashboard Cite

Dictyostelium discoideum MC2 is a temperature-sensitive motility mutant of AX3. Mutant cells are incapable of growth, phagocytosis, and migration under restrictive conditions (Kayman et al., J. Cell Biol. 92:705-711, 1982). We show here that at the restrictive temperature MC2 cells grown axenically or on bacteria synthesized excessive quantities of the lectin discoidin I. By two-dimensional gel electrophoresis and peptide mapping, the proteins overproduced by MC2 cells were indistinguishable from discoidin I synthesized at lower levels in AX3 cells. At least two of the three species of discoidin I were overproduced. This protein family constituted 9% of the total protein in cells that were incubated overnight at 27°C in axenic medium. Although MC2 cells are defective in nutrient uptake under restrictive conditions, the overproduction of discoidin I did not appear to be part of a pleiotropic response to starvation. We propose that transcription of the coordinately regulated discoidin I genes is altered in mutant cells. This alteration may be related to the motility defects manifested by MC2.

show abstract

mentioning

confidence: 72%

mentioning

confidence: 99%

See 1 more Smart Citation

Overproduction of discoidin I by a temperature-sensitive motility mutant of Dictyostelium discoideum.

Biswas¹,

Kayman²,

Clarke³

1984

Mol. Cell. Biol.

View full text Add to dashboard Cite

show abstract

“…Two independent constructs for homologous recombination were then linearized and transformed by electroporation into JH10 cells, a thymidine auxotroph (32,56 To further examine the possibility that ERK1 is essential for growth, we made an ERK1 antisense construct with the discoidin I-y (Discly) promoter, whose expression can be regulated by exogenous folate during vegetative growth (3,66). This gene is not expressed in cells grown on bacteria or in axenic culture when cells are maintained at a very low density (15,66). As the cell density increases, the concentration of a secreted protein factor, PSF, rises, and Discly expression is induced (9).…”

Section: Multicellular Development In Dictyostelium Discoideum Ismentioning

confidence: 99%

Identification and functional analysis of a developmentally regulated extracellular signal-regulated kinase gene in Dictyostelium discoideum.

Gaskins¹,

Maeda²,

Firtel³

1994

Mol. Cell. Biol.

View full text Add to dashboard Cite

We have cloned a developmentally regulated mitogen-activated protein kinase (extracellular signal-regulated kinase) from Dictyostelium discoideum designated ERK1. Using anti-pTyr antibodies, we show that ERKI is phosphorylated on tyrosine in vivo and that it will phosphorylate myelin basic protein. The (16,26). As the aggregate forms, extracellular signals produced within the organism induce cell type differentiation and regulate morphogenesis. These events lead to the production of a migrating slug followed by culmination and the generation of a mature fruiting body containing spores and stalk cells (49,50,80). Biochemical and molecular genetic analyses over the last few years have identified components required for various aspects of these processes and have led to a further understanding of the regulatory pathways controlling development. Genes encoding membrane receptors, coupled GP and Got subunits, the effectors adenylyl cyclase and phospholipase C, and the transcription factor GBF have been cloned and analyzed at a molecular level (12,17,32,65,72,81,82 the membrane to those in the nucleus is cAMP-dependent protein kinase (PKA). PKA has been shown to be essential for aggregation, cell-type-specific expression of the ecmB gene, the induction of prespore cell differentiation, and the induction of sporulation and spore cell-specific gene expression (1, 27, 35, 36, 40, 56-58, 76, 77 (8, 21-23, 61, 79, 84). In metazoans, both G protein-and tyrosine kinase-coupled receptors regulate growth responses, gene expression, and cellular differentiation via MAPK-containing pathways (2,7,11,51,60,64,83). MAPK family members have also been shown to directly phosphorylate transcription factors in mammalian cells, including Myc, Elk, and Jun proteins, leading to an increase in the rate of transcription (14,29,38,46,59,74,75).

show abstract

“…Discoidin domains, first identified in the discoidin I protein of Dictyostelium discoidium (9,10), have now been found in many secreted and transmembrane proteins, including blood coagulation factors, tyrosine kinase receptors, and proteins involved in neural development (11)(12)(13). The function of the discoidin domain is not well understood, but in some proteins it has been implicated in cell adhesion and cell signaling through protein-protein, protein-carbohydrate, or protein-lipid interactions.…”

mentioning

confidence: 99%

Defective Discoidin Domain Structure, Subunit Assembly, and Endoplasmic Reticulum Processing of Retinoschisin are Primary Mechanisms Responsible for X-linked Retinoschisis

Molday

2003

Journal of Biological Chemistry

104

136

View full text Add to dashboard Cite

Retinoschisin is a 24-kDa discoidin domain-containing protein that is secreted from photoreceptor and bipolar cells as a large disulfide-linked multisubunit complex. It functions as a cell adhesion protein to maintain the cellular organization and synaptic structure of the retina. Over 125 different mutations in the RS1 gene are associated with X-linked juvenile retinoschisis, the most common form of early onset macular degeneration in males. To identify molecular determinants important for retinoschisin structure and function and elucidate molecular and cellular mechanisms responsible for X-linked juvenile retinoschisis, we have analyzed the expression, protein folding, disulfide-linked subunit assembly, intracellular localization, and secretion of wild-type retinoschisin, 15 Cys-to-Ser variants and 12 disease-linked mutants. Our studies, together with molecular modeling of the discoidin domain, identify Cys residues involved in intramolecular and intermolecular disulfide bonds essential for protein folding and subunit assembly. We show that misfolding of the discoidin domain, defective disulfide-linked subunit assembly, and inability of retinoschisin to insert into the endoplasmic reticulum membrane as part of the protein secretion process are three primary mechanisms responsible for the loss in the function of retinoschisin as a cell adhesion protein and the pathogenesis of X-linked juvenile retinoschisis.X-linked juvenile retinoschisis (XLRS) 1 is the most common form of early onset macular degeneration in males (1, 2). It is characterized by a mild to severe decrease in visual acuity, radial streaks extending from the central retina due to a splitting of the inner retina, progressive macular atrophy, and reduction in the electroretinogram b-wave (2-5). Lesions in the peripheral retina associated with impairment in peripheral vision are observed in half the cases. During the course of the disease, complications can arise, which include retinal detachment, vitreal hemorrhaging, and neovascular glaucoma leading to a poor outcome.The RS1 gene responsible for XLRS was identified by positional cloning and found to encode a 24-kDa protein called retinoschisin, or RS1 (6), that is secreted from photoreceptor and bipolar cells as a disulfide-linked oligomeric complex (7,8).The polypeptide consists of a leader sequence with a putative signal peptidase cleavage site and a discoidin domain spanning most of the protein (6). Discoidin domains, first identified in the discoidin I protein of Dictyostelium discoidium (9, 10), have now been found in many secreted and transmembrane proteins, including blood coagulation factors, tyrosine kinase receptors, and proteins involved in neural development (11-13). The function of the discoidin domain is not well understood, but in some proteins it has been implicated in cell adhesion and cell signaling through protein-protein, protein-carbohydrate, or protein-lipid interactions. Recently, the three-dimensional crystal structures of the C2 discoidin domain of blood coagulation Factors...

show abstract

Sequence and expression of the discoidin I gene family in Dictyostelium discoideum

Cited by 172 publications

References 19 publications

Overproduction of discoidin I by a temperature-sensitive motility mutant of Dictyostelium discoideum.

Overproduction of discoidin I by a temperature-sensitive motility mutant of Dictyostelium discoideum.

Identification and functional analysis of a developmentally regulated extracellular signal-regulated kinase gene in Dictyostelium discoideum.

Defective Discoidin Domain Structure, Subunit Assembly, and Endoplasmic Reticulum Processing of Retinoschisin are Primary Mechanisms Responsible for X-linked Retinoschisis

Contact Info

Product

Resources

About