• Search Research Projects
  • Search Researchers
  • How to Use
  1. Back to previous page

Direct binding with B-Myb imposes nuclear of cytoplasmic phosphlipase A2 to regulate B-Myb-dependent gone expression

Research Project

Project/Area Number 11671871
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field 病態科学系歯学(含放射線系歯学)
Research InstitutionNagasaki University

Principal Investigator

TASHIRO Sigeki  Nagasaki University, School of Dentistry, Instructor., 歯学部, 助手 (20300882)

Co-Investigator(Kenkyū-buntansha) SUMI Tadateru  Nagasaki University, School of Dentistry, Instructor., 歯学部・附属病院, 助手 (80284701)
KATAYAMA Ikuo  Nagasaki University, School of Dentistry, Instructor., 歯学部・附属病院, 助手 (80295089)
SHIBATA Yosiyuki  Nagasaki University, School of Dentistry, Instructor., 歯学部, 助手 (20253685)
NAKAMURA Takashi  Nagasaki University, School of Dentistry, Prof., 歯学部, 教授 (30172406)
Project Period (FY) 1999 – 2000
Project Status Completed (Fiscal Year 2000)
Budget Amount *help
¥3,100,000 (Direct Cost: ¥3,100,000)
Fiscal Year 2000: ¥1,100,000 (Direct Cost: ¥1,100,000)
Fiscal Year 1999: ¥2,000,000 (Direct Cost: ¥2,000,000)
KeywordscPLA2 / CaLB domain / nuclear export signal / intramolecular interaction / localization / transcriptional factor
Research Abstract

Cytosolic phospholipase A2 (cPLA2) cleaves membrane phospholipids to release arachidonic acid, initiating lipoxygenase and cyclooxygenase pathways. Mice lacking a gene for cPLA2 exhibit impaired allergic responses and fertility, and may have defects in neuronal cell death1,2. cPLA2 is activated by cytokines, submicromolar concentrations of Ca2+ ions, and MAP kinase-mediated phosphorylation of serine residues in the protein3.4. Activated cPLA2 protein distributes preferentially to the perinuclear region of the cell4-7, where the enzyme is thought to participate in arachidonic acid release. Here we show that cPLA2 binds directly and specifically to the B-Myb transcription factor and that, as a result, cPLA2 translocates into the nucleus. Binding site analysis demonstrated that both the N-and C-termini of cPLA2 interact with the C-terminus of B-Myb. The results also demonstrate that formation of cPLA2-B-Myb complexes and translocation to the nucleus is associated with regulation of B-Myb-dependent gene expression. These findings provide new insights into the intranuclear regulation of B-Myb function by cPLA2.

Report

(3 results)
  • 2000 Annual Research Report   Final Research Report Summary
  • 1999 Annual Research Report

URL: 

Published: 1999-04-01   Modified: 2016-04-21  

Information User Guide FAQ News Terms of Use Attribution of KAKENHI

Powered by NII kakenhi