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J. Biol. Chem., Vol. 276, Issue 45, 41803-41809, November 9, 2001

This Article Full Text Full Text (PDF) All Versions of this Article: 276/45/41803    most recent M101488200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Takeda, M. Articles by Watanabe, S. Search for Related Content PubMed PubMed Citation Articles by Takeda, M. Articles by Watanabe, S. Social Bookmarking                      What's this?

Cell Cycle-dependent Interaction of Mad2 with Conserved Box1/2 Region of Human Granulocyte-Macrophage Colony-stimulating Factor Receptor Common c^*

Mitsuo Takeda^§, Naoshi Dohmae^¶, Koji Takio^¶, Ken-ichi Arai^§, and Sumiko Watanabe

From the  Department of Molecular and Developmental Biology, Institute of Medical Science, ^§ Core Research for Evolutional Science and Technology, Japan Science and Technology Corporation, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan, and the ^¶ Biomolecular Characterization Division, RIKEN (Institute of Physical and Chemical Research), 2-1, Hirosawa, Wako-shi, Saitama 351-0198, Japan

Box1 and 2 (box1/2) are conserved cytoplasmic motifs located in the membrane proximal region of cytokine receptors, including the human granulocyte-macrophage colony-stimulating factor (GM-CSF) receptor common c. Deletion of box1/2 abrogated all the examined activities of GM-CSF, and this phenomenon is explained by the loss of binding by Jak2. To test if a molecule other than Jak2 interacting with the box1/2 region plays a role in GM-CSF receptor signal transduction, we screened for molecules interacting with the box1/2 region by a pull-down assay using recombinant purified protein of GST fused with the c box1/2 region and a Ba/F3 cell lysate. The mouse homologue of Mad2 protein, which plays an important role in the M phase of the cell cycle, was revealed to associate with the box1/2 region specifically. Peptides corresponding to the box1 sequence also bound to Mad2, and mutation of the box1 decreased the Mad2 interaction. Deletion analysis indicated that interaction with box1/2 occurred through the C-terminal portion of Mad2. Mad2 is known to change affinity for binding partners cell cycle dependently. Binding affinity of Mad2 to box1/2 increased in the late M phase, suggesting the possibility that GM-CSF participates in regulation of the M phase check point through interaction with Mad2.

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