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Sci. STKE, 28 August 2007
Vol. 2007, Issue 401, p. re6
[DOI: 10.1126/stke.4012007re6]

REVIEWS

Structure and Function of the PB1 Domain, a Protein Interaction Module Conserved in Animals, Fungi, Amoebas, and Plants

Hideki Sumimoto1,2*, Sachiko Kamakura1,2, and Takashi Ito2,3

1Medical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan.
2CREST, Japan Science and Technology Agency, 5-3 Sanbancho, Chiyoda-ku, Tokyo 102-0075, Japan.
3Department of Computational Biology, Graduate School of Frontier Sciences, University of Tokyo, 5-1-5 Kashiwanoha, Kashiwa 277-8561, Japan.

Gloss: With 9 figures, four interactive structure figures, and 170 citations, this Review describes the structure-function relationships of proteins with PB1 domains. Three types of PB1-containing proteins occur: those with a type I domain, those with a type II domain, and those with both type I and type II (type I/II). The type I domain mediates interactions with proteins containing a type II domain in a canonical PB1-PB1 interaction. Interactions mediated by PB1 domains are important for organizing cell structure, for example, in polarized cells (epithelial cells and neurons) and in skeletal muscle. In addition, interactions involving PB1 domains influence the activation of mitogen-activated protein kinase signaling and activation of NADPH oxidase.

*Corresponding author. E-mail: hsumi{at}bioreg.kyushu-u.ac.jp

Citation: H. Sumimoto, S. Kamakura, T. Ito, Structure and Function of the PB1 Domain, a Protein Interaction Module Conserved in Animals, Fungi, Amoebas, and Plants. Sci. STKE 2007, re6 (2007).

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NMR Structure of the Heterodimer of Bem1 and Cdc24 PB1 Domains from Saccharomyces Cerevisiae.
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Homogeneous Time-Resolved Fluorescence Resonance Energy Transfer Assay for Measurement of Phox/Bem1p (PB1) Domain Heterodimerization.
K. Nakamura, J. S. Zawistowski, M. A. Hughes, J. Z. Sexton, L.-A. Yeh, G. L. Johnson, and J. E. Scott (2008)
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