The Krüppel traffic report: cooperative signals direct KLF8 nuclear transport.
The Krüppel traffic report: cooperative signals direct KLF8 nuclear transport.
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The Krüppel-like transcription factor (KLF) family consists of 17 distinct family members involved in the regulation of diverse cellular processes including differentiation, cell proliferation, growth-related signal transduction, angiogenesis and apoptosis (recently reviewed in [1]). In addition to their currently known biologic roles, the discovery that at least one member of the family, KLF6, can be alternatively spliced into biologically active isoforms with antagonistic functions and a distinct subcellular localization pattern [2], highlights the fact that nuclearcytoplasmic shuttling of KLF proteins may represent an additional layer of functional regulation and the possibility of an even more diverse and completely unexplored role for KLF family members in both health and disease. The study by Mehta et al.[3] on KLF8 nuclear localization provides additional and novel findings on the signals and cooperativity between them which direct subcellular trafficking of KLF family members. Prior to discussing these findings it is worthwhile to review the basic modular structure that has been “classically” described for this family. Based on sequence comparison, the modular structure is shown to be retained even in evolutionarily distant homologues including those in Zebrafish [4], Xenopus [5] and Drosophila [6]. A central feature ascribed to all KLF family members, if alternative splicing is not considered, has been their possession of three characteristic domains. The first is a highly variable N-terminal activation domain. Post-translational modifications within this domain and interactions with other proteins through this domain are believed to underlie each KLF family member’s ability to act as either an activator or repressor of transcription. Second, a C-terminal region containing three highly conserved C2H2 zinc fingers (ZFs) comprises the DNA binding domain. Finally, based originally on the presence of an enriched stretch of basic amino acids, a nuclear localization signal (NLS) region was predicted adjacent to the start of the zinc finger DNA-binding domain (Figure 1).
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影响因子：
4.8
作者：
Du, James X.;Bialkowska, Agnieszka B.;Yang, Vincent W.
通讯作者：
Yang, Vincent W.
影响因子：
20.3
作者：
Oates, AC;Pratt, SJ;Zon, LI
通讯作者：
Zon, LI
影响因子：
16
作者：
Zhao, JH;Bian, ZC;Guan, JL
通讯作者：
Guan, JL
影响因子：
12.3
作者：
Kaczynski J;Cook T;Urrutia R
通讯作者：
Urrutia R
影响因子：
8
作者：
Wang, X.;Zhao, J.
通讯作者：
Zhao, J.