TY - JOUR
T1 - LKB1 tumor suppressor protein
T2 - PARtaker in cell polarity
AU - Baas, Annette F.
AU - Smit, Linda
AU - Clevers, Hans
N1 - Funding Information:
We thank Rachel Giles for critical reading of the manuscript, and Johan Offerhaus for helpful discussions. We also thank Jeroen Kuipers and Dario Alessi for help with figure preparation. Our work is supported by the Center for Biomedical Genetics.
PY - 2004/6
Y1 - 2004/6
N2 - The LKB1 (also called serine/threonine kinase 11) tumor suppressor gene was cloned in 1998 by linkage analysis of Peutz-Jeghers cancer syndrome patients. Mammalian LKB1 has been implicated as a regulator of multiple biological processes and signaling pathways, including the control of cell-cycle arrest, p53-mediated apoptosis, Wnt signaling, transforming growth factor (TGF)-β signaling, ras-induced cell transformation, and energy metabolism. The Caenorhabditis elegans and Drosophila melanogaster LKB1 homologs, termed PAR4 and dLKB1, respectively, regulate cell polarity. Recently, mammalian LKB1 was found to be active only in a complex with two other proteins - STRAD and MO25 - and to induce complete polarization of intestinal epithelial cells in a cell-autonomous fashion. In this article, we summarize the findings regarding LKB1 over the past six years. In addition, we discuss LKB1 in polarity in the context of both the other PAR proteins and its tumor suppressive activities.
AB - The LKB1 (also called serine/threonine kinase 11) tumor suppressor gene was cloned in 1998 by linkage analysis of Peutz-Jeghers cancer syndrome patients. Mammalian LKB1 has been implicated as a regulator of multiple biological processes and signaling pathways, including the control of cell-cycle arrest, p53-mediated apoptosis, Wnt signaling, transforming growth factor (TGF)-β signaling, ras-induced cell transformation, and energy metabolism. The Caenorhabditis elegans and Drosophila melanogaster LKB1 homologs, termed PAR4 and dLKB1, respectively, regulate cell polarity. Recently, mammalian LKB1 was found to be active only in a complex with two other proteins - STRAD and MO25 - and to induce complete polarization of intestinal epithelial cells in a cell-autonomous fashion. In this article, we summarize the findings regarding LKB1 over the past six years. In addition, we discuss LKB1 in polarity in the context of both the other PAR proteins and its tumor suppressive activities.
UR - http://www.scopus.com/inward/record.url?scp=2942729619&partnerID=8YFLogxK
U2 - 10.1016/j.tcb.2004.04.001
DO - 10.1016/j.tcb.2004.04.001
M3 - Review article
C2 - 15183188
AN - SCOPUS:2942729619
SN - 0962-8924
VL - 14
SP - 312
EP - 319
JO - Trends in Cell Biology
JF - Trends in Cell Biology
IS - 6
ER -