| PKB Binding Proteins Cell, Volume 111, Issue 3, 1 November 2002, Pages 293-303 Derek P. Brazil, Jongsun Park and Brian A. Hemmings Summary Protein kinase B (PKB) has emerged as the focal point for many signal transduction pathways, regulating multiple cellular processes such as glucose metabolism, transcription, apoptosis, cell proliferation, angiogenesis, and cell motility. In addition to acting as a kinase toward many substrates involved in these processes, PKB forms complexes with other proteins that are not substrates, but rather act as modulators of PKB activity and function. In this review, we discuss the implications of these data in understanding the multitude of functions predicted for PKB in cells. Summary | Full Text | PDF (335 kb) |
| Akt is TCL-ish: implications for B-cell lymphoma Trends in Immunology, Volume 24, Issue 3, 1 March 2003, Pages 104-108 Michael R. Gold Abstract The (T-cell leukemia 1) protooncogene is highly expressed in many human B-cell leukemias and two recent papers show that overexpression causes rapid development of B-cell lymphomas in mice. Other recent work showing that the TCL1 protein enhances the activation of the pro-survival kinase Akt has revealed a potential mechanism underlying the development of B-cell leukemias and raised new questions about the regulation of Akt. Abstract | Full Text | PDF (575 kb) |
| Krüppel-like factor 5 Is Essential for Blastocyst Development and the Normal Self-Renewal of Mouse ESCs Cell Stem Cell, Volume 3, Issue 5, 6 November 2008, Pages 555-567 Masatsugu Ema, Daisuke Mori, Hitoshi Niwa, Yoshikazu Hasegawa, Yojiro Yamanaka, Seiji Hitoshi, Junsei Mimura, Yoh-ichi Kawabe, Tomohiro Hosoya, Masanobu Morita, Daisuke Shimosato, Kazuhiko Uchida, Norio Suzuki, Jun Yanagisawa, Kazuhiro Sogawa, Janet Rossant, Masayuki Yamamoto, Satoru Takahashi and Yoshiaki Fujii-Kuriyama Summary The transcription factor has demonstrated activity in the reprogramming of somatic cells to a pluripotent state, but the molecular mechanism of this process remains unknown. It is, therefore, of great interest to understand the functional role of Klf4 and related genes in ESC regulation. Here, we show that homozygous disruption of results in the failure of ESC derivation from ICM cells and early embryonic lethality due to an implantation defect. KO ESCs show increased expression of several differentiation marker genes and frequent, spontaneous differentiation. Conversely, overexpression of in ESCs suppressed the expression of differentiation marker genes and maintained pluripotency in the absence of LIF. Our results also suggest that regulates ESC proliferation by promoting phosphorylation of Akt1 via induction of Tcl1. These results, therefore, provide new insights into the functional and mechanistic role of in regulation of pluripotency. Summary | Full Text | PDF (1102 kb) |
Copyright © 2000 Cell Press. All rights reserved.
Molecular Cell, Volume 6, Issue 2, 395-407, 1 August 2000
doi:10.1016/S1097-2765(00)00039-3
Article
Jarmo Laine1, Gerald Künstle1, Toshiyuki Obata2, Ma Sha3 and Masayuki Noguchi1, §, *, 
1 Department of Medicine, Division of Immunology, Beth Israel Deaconess Medical Center and, Harvard Medical School , Boston, Massachusetts 02215, USA
2 Department of Medicine, Division of Signal Transduction, Beth Israel Deaconess Medical Center and, Harvard Medical School , Boston, Massachusetts 02215, USA
3 Ciphergen Biosystems, Incorporated, Palo Alto, California 94306, USA
Corresponding author: Masayuki Noguchi, 617 632 0521 (phone), 617 632 0160 (fax)Human T cell prolymphocytic leukemia can result from chromosomal translocations involving 14q32.1 or Xq28 regions. The regions encode a family of protooncogenes (TCL1, MTCP1, and TCL1b) of unknown function. In yeast two-hybrid screening, we found that TCL1 interacts with Akt. All TCL1 isoforms bind to the Akt pleckstrin homology domain. Both in vitro and in vivo TCL1 increases Akt kinase activity and as a consequence enhances substrate phosphorylation. In vivo, TCL1 stabilizes the mitochondrial transmembrane potential and enhances cell proliferation and survival. In vivo, TCL1 forms trimers, which associate with Akt. TCL1 facilitates the oligomerization and activation of Akt. Our data show that TCL1 is a novel Akt kinase coactivator, which promotes Akt-induced cell survival and proliferation.