제 249회 NEBS Monthly meeting 개최를 다음과 같이 알려드립니다.
일시: 2016년 9월 29일 (목요일) 오후 6시 30분
(7시 이후 엘레베이터 이용이 제한되니 가급적 7시 이전에 오시길 부탁드리며, 7시 이후의 경우 Security guard에게 미팅 참석 여부를 확인 후 엘리베이터 이용을 부탁해 주세요.)
New Research Building, 10th floor conference room
77 Ave Louis Pasteur, Boston, MA 02115
6:20 - 7:00 저녁식사
7:00 - 7:10 공지사항
7:10 – 7:50 학술 세미나 1 -
“The m6A Methyltransferase METTL3 Promotes Translation in Human Cancer Cells”
By Junho Choe, Ph. D (Boston Children’s Hospital)
7:50 - 8:30 학술 세미나 2 –
“Flower (Enzyme) + Pig (Glycan) + Human (Antibody) + Mouse (Immunology) = ? ”
By Hee-Jin Jeong, Ph. D (Dana-Farber Cancer Institute)
- 11:00 뒷풀이 (Longwood Grill)
미팅 참석시 주차는 375 Longwood garage (http://www.masco.org/directions/375-longwood-garage)를 이용해주시기 바랍니다. 당일날 참석인원 확인용지에 주소를 기입해주시면 주차 지원비 7불을 check 으로 발송해 드리겠습니다 (미팅에 오실때 카풀을 하시는 분들을우선적으로 지원해드리기로 되어 있습니다).
회원 여러분들의 많은 참여 부탁드립니다.
세미나 초록은 아래를 참고해 주시길 바랍니다.
Title: The m6A Methyltransferase METTL3 Promotes Translation in Human Cancer Cells
METTL3 is an RNA methyltransferase implicated in mRNA biogenesis, decay, and translation control through N6-methyladenosine (m6A) modification. Here we find that METTL3 promotes translation of certain mRNAs including epidermal growth factor receptor (EGFR) and the Hippo pathway effector TAZ in human cancer cells. In contrast to current models that invoke m6A reader proteins downstream of nuclear METTL3, we find METTL3 associates with ribosomes and promotes translation in the cytoplasm.
METTL3 depletion inhibits translation, and both wild-type and catalytically inactive METTL3 promote translation when tethered to a reporter mRNA. Mechanistically, METTL3 enhances mRNA translation through an interaction with the translation initiation machinery. METTL3 expression is elevated in lung adenocarcinoma and using both loss- and gain-of-function studies, we find that METTL3 promotes growth, survival, and invasion of human lung cancer cells. Our results uncover an important role of METTL3 in promoting translation of oncogenes in human lung cancer.
Title: Flower (Enzyme) + Pig (Glycan) + Human (Antibody) + Mouse (Immunology) = ?
Our group recently developed a unique and powerful fluoroimmunosensor named Quenchbody (Q-body) that works on the novel principle of antigen-dependent removal of quenching effect on a fluorophore. The outstanding advantage of Q-body assay is its simplicity, which can be carried out by just mixing the Q-body with antigen and measuring its fluorescence, while almost all the traditional immunoassays require several incubation/washing steps. Using this convenient method, we have successfully quantified various target antigens including narcotics such as morphine and influenza hemagglutinin. In particular, as a model Q-body, we constructed several types of Q-body against osteocalcin, which is a bone disease marker, with different numbers of fluorophore as well as the different protein formats. Moreover, using this Q-body, cellular imaging of osteocalcin produced by differentiated osteoblast cells was successfully accomplished. Due to its simplicity and versatility, Q-body assay is expected to have a range of applications, from in vitro diagnostics to imaging of various targets in situ.