京都大学 · 生化学・遺伝学・分子生物学
白川正博教授の研究室は、タンパク質修飾とその機能解明を柱として、ユビキチン化やSUMO化といった翻訳後修飾が細胞内シグナル伝達に果たす役割を、主にNMR分光法と分子動力学シミュレーションを用いて解明しています。特に、ユビキチン・ユビキチン様分子とそのリセプターの特異的相互作用の構造的基盤を解明しており、がんや神経変性疾患のメカニズム解明に寄与する基盤研究を推進しています。また、ナノスケールpHセンサーの開発やATPの非共有結合的相互作用の解明といった、バイオ・ナノ分野とのクロスオーバー研究も展開しています。
Figures are computed from collected data and may differ slightly.
Ubiquitination, a modification in which single or multiple ubiquitin molecules are attached to a protein, serves as a signalling function that controls a wide variety of cellular processes. To date, two major forms of polyubiquitin chain have been functionally characterized, in which the isopeptide bond linkages involve Lys48 or Lys63. Lys48-linked polyubiquitin tagging is mostly used to target proteins for degradation by the proteasome, whereas Lys63-linked polyubiquitination has been linked to
Nanoscale measurements provide insight into the nano world. For instance, nanometric spatiotemporal distribution of intracellular pH is regulated by and regulates a variety of biological processes. However, there is no general method to fabricate nanoscale pH sensors. Here, we, to endow pH-sensing functions, tailor the surface properties of a fluorescent nanodiamond (FND) containing nitrogen-vacancy centers (NV centers) by coating the FND with an ionic chemical layer. The longitudinal relaxation
Adenosine triphosphate (ATP) is an immensely well-studied metabolite serving multiple key biochemical roles as the major chemical energy currency in living systems, a building block of ribonucleic acids, and a phosphoryl group donor in kinase-mediated signaling. Intriguingly, ATP has been recently proposed to act as a <i>hydrotrope</i> that inhibits aggregation of amyloidogenic proteins; however, the underlying mechanism and the general physicochemical effect that coexistence with ATP exerts on
Ubiquitination, a modification in which single or multiple ubiquitin molecules are attached to a protein, serves signaling functions that control several cellular processes. The ubiquitination signal is recognized by downstream effectors, many of which carry a ubiquitin-interacting motif (UIM). Such interactions can be modulated by regulators carrying a ubiquitin-like (UbL) domain, which binds UIM by mimicking ubiquitination. Of them, HR23B regulates the proteasomal targeting of ubiquitinated su
Post-translational modification by small ubiquitin-like modifier (SUMO) proteins has been implicated in the regulation of a variety of cellular events. The functions of sumoylation are often mediated by downstream effector proteins harboring SUMO-interacting motifs (SIMs) that are composed of a hydrophobic core and a stretch of acidic residues. MBD1-containing chromatin-associated factor 1 (MCAF1), a transcription repressor, interacts with SUMO-2/3 and SUMO-1, with a preference for SUMO-2/3. We
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