Transcription factor phosphorylation by the DNA-dependent protein kinase.
نویسندگان
چکیده
21. Geisler, R., Bergmann, A,, Hiromi, Y. and NussleinVolhard, C. (1992) Cell 71,613-621 Inoue, J.-I., Kerr, L. D., Kakizuka, A. and Verma, I. M. (1992) Cell 68, 1109-1 120 Liou, H.-C., Nolan, G. P., Ghosh, S., Fujita, T. and Baltimore, D. (1992) EMBO J. 11, 3003-3009 Wulczyn, F. G., Naumann, M. and Scheidereit, C. (1992) Nature (London) 358,597-599 Bours, V., Franzoso, G., Azarenko, V., Park, S., Kanno, T., Brown, K. and Siebenlist, U. (1993) Cell
منابع مشابه
Effects of Antiproliferative Protein (APP) on Modulation of Cytosolic Protein Phosphorylation of Prostatic Carcinoma Cell Line LNCaP
Antiproliferative protein (APP) isolated from conditioned media of two androgen-independent prostatic carcinoma cell lines, PC3 and Du-145 was shown to inhibit selectively cell proliferation of androgen-dependent prostate cancer cell line LNCaP in a dose dependent manner. This protein was further purified with HPLC using hydrophobic interaction column (phenyl 5PW) and was used to study the modu...
متن کاملThe Role of Tumor Protein 53 Mutations in Common Human Cancers and Targeting the Murine Double Minute 2–P53 Interaction for Cancer Therapy
The gene TP53 (also known as protein 53 or tumor protein 53), encoding transcription factor P53, is mutated or deleted in half of human cancers, demonstrating the crucial role of P53 in tumor suppression. There are reports of nearly 250 independent germ line TP53 mutations in over 100 publications. The P53 protein has the structure of a transcription factor and, is made up of several domains. T...
متن کاملRegulation of Genotoxic Stress Response by Homeodomain-interacting Protein Kinase 2 through Phosphorylation of Cyclic AMP Response Element-binding Protein at Serine 271
CREB (cyclic AMP response element-binding protein) is a stimulus-induced transcription factor that plays pivotal roles in cell survival and proliferation. The transactivation function of CREB is primarily regulated through Ser-133 phosphorylation by cAMP-dependent protein kinase A (PKA) and related kinases. Here we found that homeodomain-interacting protein kinase 2 (HIPK2), a DNA-damage respon...
متن کاملTHE EFFECT OF THEOPHYLLINE ON THE KINETICS OF cAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT, cAMP, PROTEIN KINASE INHIBITOR AND THEIR RELATIONSHIP IN LUNG TISSUE
We have investigated the effect of theophylline on the kinetics of the catalytic subunit of protein kinase and related factors in lung tissue. The results show that the point of highest concentration of the C subunit of protein kinase which is active in casein phosphorylation is at 3h of incubation time, but in the presence of 100 Ilg/ InL and 10µg/mL theophylline, this is shifted to I.S an...
متن کاملDown-regulation of histone H2B by DNA-dependent protein kinase in response to DNA damage through modulation of octamer transcription factor 1.
Cells respond to double-stranded DNA breaks (DSBs) by pausing cell cycle progression to allow the repair machinery to restore genomic integrity. DNA-dependent protein kinase (DNA-PK), comprising a large catalytic subunit (DNA-PK(cs)) and the Ku antigen regulatory subunit (Ku70/Ku80), is activated in response to DSBs and is required for DNA repair through the nonhomologous end-joining pathway. H...
متن کاملPhosphorylation of Staphylococcus aureus Protein-Tyrosine Kinase Affects the Function of Glucokinase and Biofilm Formation
Background: When Staphylococcus aureus is grown in the presence of high concentration of external glucose, this sugar is phosphorylated by glucokinase (glkA) to form glucose-6-phosphate. This product subsequently enters into anabolic phase, which favors biofilm formation. The presence of ROK (repressor protein, open reading frame, sugar kinase) motif, phosphate-1 and -2 sites, and tyrosine kina...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Biochemical Society transactions
دوره 21 4 شماره
صفحات -
تاریخ انتشار 1993