Intranuclear appearance of the phosphorylated form of cytoskeleton-associated 350-kDa proteins in U1-ribonucleoprotein regions after growth stimulation of fibroblasts
| Autor: | Tokiko Nakayama, Chikako Sato, Yoshinari Takasaki, Shunichi Hirose, Kimiko Nishizawa, Hiromu Nakamura, Kiyoshi Nose |
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| Rok vydání: | 1986 |
| Předmět: |
medicine.drug_class
Biology Monoclonal antibody Cell Line Antibody Specificity Proto-Oncogene Proteins medicine Animals Phosphorylation RNA Processing Post-Transcriptional Ribonucleoprotein Cell Nucleus Messenger RNA Multidisciplinary MRNA modification Cell Cycle Antibodies Monoclonal Phosphoproteins Molecular biology Cell Compartmentation Rats Molecular Weight Cell nucleus medicine.anatomical_structure Gene Expression Regulation Ribonucleoproteins Cytoplasm Polyclonal antibodies biology.protein Microtubule-Associated Proteins Small nuclear ribonucleoprotein Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences. 83:7287-7291 |
| ISSN: | 1091-6490 0027-8424 |
| Popis: | Cytoskeleton-associated 350-kDa and 80-kDa polypeptides, which were immunoprecipitated with polyclonal antibody against microtubule-associated protein 1 (MAP-1), were rapidly phosphorylated on mitogenic stimulation of quiescent fibroblasts with serum or growth factors. The enhanced phosphorylation was evident within 5 min and reached a maximum 2 hr after the stimulation. Phosphorylated MAP-1 analogues were first detected in the cytoplasm around the microtubule-organizing center and then in the nucleus by immunofluorescent staining with a monoclonal antibody that recognized the phosphorylated form of MAP-1. The monoclonal antibody reacted with the 350-kDa protein in immunoblot analysis and immunostained intranuclear speckles; both immunoreactions were abolished by treatment with alkaline or acid phosphatase. The nuclear speckles stained by the monoclonal antibody were also stained by anti-U1 small nuclear ribonucleoprotein antibodies on double immunofluorescence, suggesting that the stained regions are sites of maturation of messenger RNA. These results support the idea that part of the cytoskeleton-associated 350-kDa protein is phosphorylated and transferred to the nuclear region of mRNA modification as a common early process after growth stimulation. |
| Databáze: | OpenAIRE |
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