Mammalian NDR/LATS protein kinases in hippo tumor suppressor signaling

The NDR/LATS family of kinases is a subgroup of the AGC group of protein kinases and is conserved from lower eukaryotes to humans. Like other AGC kinases, NDR/LATS kinases require phosphorylation of conserved Ser/Thr residues for activation. On the one hand, binding of the coactivator MOB to NDR/LAT...

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Bibliographic Details
Published in:BioFactors (Oxford) 2009-07, Vol.35 (4), p.338-345
Main Authors: Hergovich, Alexander, Hemmings, Brian A.
Format: Article
Language:English
Subjects:
Adaptor Proteins, Signal Transducing - physiology
Animals
Cell Cycle Proteins - physiology
Drosophila Proteins - physiology
Gene Expression Regulation
Genes, Tumor Suppressor - physiology
Humans
Intracellular Signaling Peptides and Proteins - physiology
MOB/Mps one binder protein
MST/mammalian serine/threonine sterile 20-like kinase
Neurofibromin 2 - physiology
Nuclear Proteins - physiology
Protein-Serine-Threonine Kinases - physiology
Signal Transduction - physiology
STK38/STK38L
Transcription Factors - physiology
Tumor Suppressor Proteins - physiology
tumor suppressor/proto-oncogene
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Summary:The NDR/LATS family of kinases is a subgroup of the AGC group of protein kinases and is conserved from lower eukaryotes to humans. Like other AGC kinases, NDR/LATS kinases require phosphorylation of conserved Ser/Thr residues for activation. On the one hand, binding of the coactivator MOB to NDR/LATS allows autophosphorylation. On the other hand, MST kinases directly phosphorylate NDR/LATS kinases. In addition to our understanding of the molecular activation mechanisms, recent studies have shown that LATS kinases play a central role in Hippo/SWH (Salvador/Warts/Hippo) tumor suppressor pathways, which coordinate cell proliferation and apoptosis by regulating proto‐oncogenes, such as YAP and TAZ. In this review, we summarize current knowledge of Merlin/MST/SAV/MOB/LATS/NDR/YAP/TAZ networks (also termed mammalian Hippo signaling) and their roles in mammalian cellular transformation. © 2009 International Union of Biochemistry and Molecular Biology, Inc.
ISSN:0951-6433
1872-8081
DOI:10.1002/biof.47