Casein Kinase II-mediated Phosphorylation of the C Terminus of Sp1 Decreases Its DNA Binding Activity
238
TL;DR: It is demonstrated that casein kinase II (CKII) is able to phosphorylate the C terminus of Sp1 and results in a decrease in DNA binding activity, which suggests that CKII may be responsible for the observed regulation of Sp 1.
read more
About: This article is published in Journal of Biological Chemistry. The article was published on 23 May 1997. and is currently open access. The article focuses on the topics: Casein kinase 2 & Phosphorylation.
read more
Chat with Paper
AI Agents for this Paper
Find similar papers on Google Scholar, PubMed and Arxiv
Write a critical review of this paper
Analyze citations of this paper to find unaddressed research gaps
Citations
One-thousand-and-one substrates of protein kinase CK2?
Flavio Meggio,Lorenzo A. Pinna +1 more
TL;DR: An analysis of 308 sites phosphorylated by CK2 highlights the paramount relevance of negatively charged side chains that are (by far) predominant over any other residues at positions n+3 (the most crucial one), n+1, and n+2.
1.3K
Sp1 and Krüppel-like factor family of transcription factors in cell growth regulation and cancer
TL;DR: The Sp/KLF family contains at least twenty identified members which include Sp1‐4 and numerous krüppel‐like factors; thus, the family is involved in several aspects of tumorigenesis.
1K
Regulation of the activity of Sp1-related transcription factors
Peter Bouwman,Sjaak Philipsen +1 more
TL;DR: The connection between functional specificity and biochemical properties including glycosylation, phosphorylation and acetylation of Sp1-related factors are focused on.
485
Sp1 and the ‘hallmarks of cancer’
TL;DR: A more complete understanding of the function of Sp1 in cancer is required to validate its potential as a therapeutic target, and the evidence suggesting that Sp1 is highly regulated by post‐translational modifications that positively and negatively affect the activity of Sp 1 on a wide array of genes is reviewed.
482
Sp1 Phosphorylation and Its Regulation of Gene Transcription
TL;DR: Recent developments in the understanding of the role of posttranslational modifications influencing Sp1-dependent transcription are discussed, focusing mainly on phosphorylation.
346
References
The structure and regulation of protein phosphatases
TL;DR: Four major serine/threonine-specific protein phosphatase catalytic subunits are present in the cytoplasm of animal cells and have broad and overlapping specificities in vitro, and account for virtually all measurable activity in tissue extracts toward a variety of phosphoproteins that regulate metabolism, muscle contractility, and other processes.
2.5K
Zinc finger-DNA recognition: crystal structure of a Zif268-DNA complex at 2.1 A.
Nikola P. Pavletich,Carl O. Pabo +1 more
TL;DR: The crystal structure of a complex containing the three zinc fingers from Zif268 and a consensus DNA-binding site has been determined at 2.1 angstroms resolution and refined to a crystallographic R factor of 18.2 percent.
2.2K
Isolation of cDNA encoding transcription factor Sp1 and functional analysis of the DNA binding domain.
TL;DR: It is found that purified Sp1 requires Zn(II) for sequence-specific binding to DNA, and it is likely that Sp1 interacts with DNA by binding of the Zn (II) fingers.
1.6K
Analysis of Sp1 in vivo reveals mutiple transcriptional domains, including a novel glutamine-rich activation motif
Albert J. Courey,Robert Tjian +1 more
TL;DR: Drosophila tissue culture cells provide an Sp1-deficient background and have been used in a complementation assay to identify functional domains of human transcription factor Sp1, and it is proposed that these glutamine-rich domains represent a novel structural motif for transcriptional activation.
1.4K