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작성자 관리자 작성일11-03-23 10:46 조회4,495회 댓글0건



일시 : 2011. 3. 24 (목) 17:00

장소 : 강원대학교 자연과학대학 5호관 101호 세미나실

TITLE : Functional Roles of O-GlcNAc Modification on Nucleocytoplasmic Proteins

SPEAKER : 조 진 원 교수 (연세대학교 대학원 오믹스 융합과학과)

     Professor, Yonsei University, Department of Biology
     Vice President, Korean Society for Glycosciences
     National Representative of International Glycoconjugates Organization
     Chair, Education Committee, KSMCB

     Secretary General, Korean Society for Glycosciences

     Secretary General, Korean Society for Molecular and Cellular Biology

     State University of New York, Stony Brook, PostDoc


O-GlcNAc modification is a new form of nucleocytoplasmic protein glycosylation found in all eukaryotes.  Like phosphorylation, this modification is ubiquitous and very dynamic. The O-GlcNAc is modified at serine and threonine residues of the targeted proteins and its dynamic modification is caused by the action of O-GlcNAc transferase (OGT) and O-GlcNAcase. Because O-GlcNAc modification sites are shared with phosphorylation, this modification appears to have a ‘yin-yang’ relationship with phosphorylation with many regulatory proteins and to play an important role in regulation of protein function. More than 100 proteins have been identified as O-GlcNAc modified proteins and these proteins can be categorized into mainly three groups; nuclear proteins (ex. many transcription factors, chromatin proteins, oncogene proteins, etc), cytoskeletal proteins (ex. cytokeratins, MAPs, tau, etc) and other proteins (ex. β-amyloid precursor proteins, heat shock proteins, etc). Main focus in my lab is to identify more O-GlcNAcylated glycoproteins related to cellular function and to elucidate the function of this modification and its attachment sites. Recently we found function and attachment sites of O-GlcNAc modification in p53 and NF-kB. In the case of p53, O-GlcNAc modification increases life span of p53 as O-GlcNAcylated p53can evade from ubiquitination and proteolysis via proteasome.  Its attachment site was identified using quadrupole time-of flight tandem mass spectrometry (Q-TOF MS) and it turned out that the site was shared with phosphorylation by COP9 signalosome.  In the case of NF-kB, O-GlcNAc modification caused to detach fromI-kB without any signal, and O-GlcNAcylated NF-kB stayed inside nucleus longer and showed more transcriptional activation.  More O-GlcNAcylated NF-kB existed in various organs from diabetic mouse, and this may indicate that O-GlcNAcylated NF-kB would be an important factor to cause complexion of diabetes. Research of O-GlcNAc modification is rapidly growing field and especially O-GlcNAc modification is very important in diabetes, neural disease and development, and many cancer.

KEYWORDS: O-GlcNAc, diabetes, p53, NF-kB
[이 게시물은 스크립스코리아님에 의해 2018-09-14 15:52:12 공지사항에서 이동 됨]


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