The family feud: turning off Sp1 by Sp1-like KLF proteins. Biochem J 2005 Nov 15;392(Pt 1):1-11
Date
11/04/2005Pubmed ID
16266294Pubmed Central ID
PMC1317658DOI
10.1042/BJ20051234Scopus ID
2-s2.0-28044461728 (requires institutional sign-in at Scopus site) 176 CitationsAbstract
Sp1 is one of the best characterized transcriptional activators. The biological importance of Sp1 is underscored by the fact that several hundreds of genes are thought to be regulated by this protein. However, during the last 5 years, a more extended family of Sp1-like transcription factors has been identified and characterized by the presence of a conserved DNA-binding domain comprising three Krüppel-like zinc fingers. Each distinct family member differs in its ability to regulate transcription, and, as a consequence, to influence cellular processes. Specific activation and repression domains located within the N-terminal regions of these proteins are responsible for these differences by facilitating interactions with various co-activators and co-repressors. The present review primarily focuses on discussing the structural, biochemical and biological functions of the repressor members of this family of transcription factors. The existence of these transcriptional repressors provides a tightly regulated mechanism for silencing a large number of genes that are already known to be activated by Sp1.
Author List
Lomberk G, Urrutia RAuthors
Gwen Lomberk PhD Adjunct Professor in the Institute for Health and Humanity department at Medical College of WisconsinRaul A. Urrutia MD Center Director, Professor in the Surgery department at Medical College of Wisconsin
MESH terms used to index this publication - Major topics in bold
Amino Acid SequenceAnimals
Gene Expression Regulation
Kruppel-Like Transcription Factors
Molecular Sequence Data
Repressor Proteins
Sp1 Transcription Factor
