Regulatory mechanism for intracellar traficking of the membrane-bound NEU3 sialidase

2014 Fiscal Year Final Research Report

• Project/Area Number: 24570142
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Structural biochemistry
• Research Institution: Miyagi Prefectural Hospital Organization Miyagi Cancer Center
• Principal Investigator: YAMAGUCHI Kazunori 地方独立行政法人宮城県立病院機構宮城県立がんセンター(研究所), その他部局等, 研究員 (80373215)
• Co-Investigator(Renkei-kenkyūsha): TANAKA Nobuyuki 宮城県立がんセンター研究所, 部長 (60280872) ; MIYAGI Taeko 東北薬科大学, 分子生体膜研究所, 教授 (50006110)
• Project Period (FY): 2012-04-01 – 2015-03-31
• Keywords: シアリダーゼ / ガングリオシド / 細胞内輸送 / シグナル伝達

Outline of Final Research Achievements

We previously found that activation of EGF receptor signaling triggers translocation of the membrane-bound NEU3 sialidase from cytoplasm to cell membrane, which had not been reported for other glycoenzymes. To gain an insight into the molecular mechanism underlying NEU3 intracellular trafficking, we attempted to identify proteins which can interact with NEU3 in cells. We identified evectin, CAMK1G, MAP1A, and ITM2C as potent candidates for NEU3-binding proteins and got structural information about the interaction. These results could provide an important clue for understanding how NEU3 modulates signal transductions and subsequently affects on pathological conditions such as cancer or diabetes.

Free Research Field

分子細胞生物学