rZIP, a RING-leucine zipper protein that regulates cell fate determination during Dictyostelium development
| Autor: | Balint-Kurti, P., Ginsburg, G., Kimmel, A. R., Octavio Miguel Rivero-Lezcano |
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| Rok vydání: | 1997 |
| Předmět: |
Leucine Zippers
Time Factors Recombinant Fusion Proteins Genes Fungal Molecular Sequence Data fungi Cell Differentiation Spores Fungal beta-Galactosidase Gene Expression Regulation Fungal Calcium-Calmodulin-Dependent Protein Kinases Animals Dictyostelium Amino Acid Sequence Phosphorylation Promoter Regions Genetic Dimerization Molecular Biology Transcription Factors Developmental Biology |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 1477-9129 0950-1991 |
| Popis: | rZIP is an approx. 32 kDa, multi-domain protein of Dictyostelium discoideum whose structural motifs include a RING (zinc-binding) domain, a leucine zipper, a glutamine repeat, an SH3-binding region and a consensus phosphorylation site for MAP kinase. In vitro, rZIP forms homodimers and interacts specifically with the SH3 domain(s) of the Nck adaptor protein. rZIP is expressed maximally during cell differentiation at approximately equivalent levels in all cells. Disruption of the rZIP gene rzpA results in altered cellular aggregation, impaired slug migration, and aberrant patterning of prespore and prestalk cells, the major progenitor classes. In rzpA− strains, presporespecific genes are overexpressed and prestalk expression zones are reduced. Conversely, constitutive overexpression of rzpA markedly decreases prespore-specific gene expression and significantly increases the expression of prestalk-specific genes. Further, induced transdifferentiation of prespore cells into prestalk cells is inhibited in rzpA− slugs. In light of these patterning defects, we suggest that the RING/zipper protein rZIP plays an important role in early cell fate decisions in Dictyostelium, acting as a positive regulator of prestalk differentiation and an inhibitor of prespore differentiation. |
| Databáze: | OpenAIRE |
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