RIKEN Center for Life Science Technologies


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Labs & Technologies

Post-transcriptional Control Research Unit

Exploring the RNP complexes involved in the regulation of protein synthesis.


* Due to the reorganization starting as new centers in April 2018, the research activities of this laboratory are handed over to the Center for Biosystems Dynamics Research. As for the latest information, please see the following URL below.
> The webpage of Laboratory for Nonnatural Amino Acid Technology, Center for Biosystems Dynamics Research

Unit Leader
Motoaki Wakiyama  Ph.D.

1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan


Research Area

Control of cellular function and cell fate determination is dependent on the regulation of gene expression. The eukaryotic gene expression was thought to be mainly regulated at transcription level. However, based on the accumulation of the knowledge in microRNA function, it is now believed that post-transcriptional control of gene expression is much more diverse and intricate than previously thought, and is extensively involved in numerous diseases. Post-transcriptional gene regulation is mediated by a number of RNA-binding proteins (RBP), RBP-binding proteins and non-coding regulatory RNAs. These factors associate with the target mRNA molecule and form a huge mRNP complex. We aim to uncover the molecular mechanism of mRNA fate determination, by developing a novel method for the investigation of the architecture and function of mRNPs.

Main Publications List


MicroRNA-mediated deadenylation in a mammalian cell-free system.

Wakiyama M, Yokoyama S.
Methods Mol Biol, 1125, 341-351 (2014).

Posttranscriptional Control of Protein Synthesis in Drosophila S2 Cell-Free System

Wakiyama, M. and Yokoyama, S.
Methods Mol Biol, 1118, 257-266 (2014).

Tetrameric interaction of the ectoenzyme CD38 on the cell surface enables its catalytic and raft-association activities.

Hara-Yokoyama M, Kukimoto-Niino M, Terasawa K, Harumiya S, Podyma-Inoue KA, Hino N, Sakamoto K, Itoh S, Hashii N, Hiruta Y, Kawasaki N, Mishima-Tsumagari C, Kaitsu Y, Matsumoto T, Wakiyama M, Shirouzu M, Kasama T, Takayanagi H, Utsunomiya-Tate N, Takatsu K, Katada T, Hirabayashi Y, Yokoyama S, Yanagishita M.
Structure, 20(9), 1585-1592 (2012).

Structural basis for the altered drug sensitivities of non-small cell lung cancer-associated mutants of human epidermal growth factor receptor.

Yoshikawa S, Kukimoto-Niino M, Parker L, Handa N, Terada T, Fujimoto T, Terazawa Y, Wakiyama M, Sato M, Sano S, Kobayashi T, Tanaka T, Chen L, Liu ZJ, Wang BC, Shirouzu M, Kawa S, Semba K, Yamamoto T, Yokoyama S.
Oncogene, 32(1), 27-38 (2012).

Structures of the first and second double-stranded RNA-binding domains of human TAR RNA-binding protein.

Yamashita S, Nagata T, Kawazoe M, Takemoto C, Kigawa T, Güntert P, Kobayashi N, Terada T, Shirouzu M, Wakiyama M, Muto Y, Yokoyama S.
Protein Sci, 20(1), 118-130 (2011).

Alteration of enzymatic properties of cell-surface antigen CD38 by agonistic anti-CD38 antibodies that prolong B cell survival and induce activation.

Hara-Yokoyama M, Kimura T, Kaku H, Wakiyama M, Kaitsu Y, Inoue M, Kusano S, Shirouzu M, Yokoyama S, Katada T, Hirabayashi Y, Takatsu K, Yanagishita M.
Int Immunopharmacol, 8(1), 59-70 (2008).

Let-7 microRNA-mediated mRNA deadenylation and translational repression in a mammalian cell-free system.

Wakiyama M, Takimoto K, Ohara O, Yokoyama S.
Genes Dev, 21(15), 1857-1862 (2007).

Cell-free translation system from Drosophila S2 cells that recapitulates RNAi.

Wakiyama M, Kaitsu Y, Yokoyama S.
Biochem Biophys Res Commun, 343(4), 1067-1071 (2006).

>>>ALL Publications

Member  *concurrent

CLST was reorganized into three centers according to the RIKEN 4th Medium-Term Plan from April 1, 2018.

> The webpage of Laboratory for Nonnatural Amino Acid Technology, Center for Biosystems Dynamics Research [http://www.bdr.riken.jp/en/research/labs/sakamoto-k/index.html]