Dr. Shih, Hsiu-Ming 施修明 博士

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Dr. Shih, Hsiu-Ming
施修明 博士

Research Fellow
研究員

  • Ph.D. Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota

  • 2789-9060 (Lab) (Room No: N605)
  • 2652-3520 (Office)
  • 2782-7654 (Fax)
Specialty:
  • Protein-protein Interaction & Modification
  • Cancer Cell Signaling
  • Transcriptional Control

RESEARCH

Wrestling with SUMO and other protein modifications

 

SUMO modification is emerging as an important post-translational control of cellular events. While many SUMO-modified transcription factors and coactivators have been identified, little is known about the mechanism underlying SUMO-elicited protein-protein interaction and regulation. In past few years, my lab has focused on the moelcular mechanisms of Daxx protein in transcriptional control and sumoylation via a SUMO-interacting motif. We further investigate protein phosphorylation, acetylation and other modifications controlling protein sumoylation. In addition, we have recently identified several SUMO-modified factors associated with signal transduction, cell cycle, cell mobility, and viral infection. Studies are undergoing to dissect the functional significances of these factors in SUMO modification and explore the underlying mechanisms as to how cells modulate the levels of sumoylated factors in response to distinct intracellular milieu.

研究介紹

小泛素修飾分子參與轉錄調控、細胞分裂、移動及病毒感染

 

本實驗室過去幾年積極從事小泛素SUMO調節基因轉錄研究發現,Daxx蛋白質會與SUMO修飾過的轉錄因子與輔因子相結合進而抑制基因轉錄。我們更進一步證明了Daxx是透過其SUMO結合模體(SUMO-interacting motif)與SUMO部分的交互作用而調控這些分子的轉錄活性。目前我們進一步探討細胞透過磷酸化、乙醯化及其它的修飾調控小泛素修飾化蛋白質。

除了基因轉錄外,我們也發現有許多細胞蛋白質參與訊息傳遞、細胞分裂、移動及病毒蛋白質會被SUMO修飾或與SUMO結合。實驗室正積極地研究這些蛋白分子與SUMO相結合或修飾的機轉及其在生理與疾病上的重要性。

HIGHLIGHT 重要成果

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