File Download

There are no files associated with this item.

  • Find it @ UNIST can give you direct access to the published full text of this article. (UNISTARs only)
Related Researcher

서판길

Suh, Pann-Ghill
Read More

Views & Downloads

Detailed Information

Cited time in webofscience Cited time in scopus
Metadata Downloads

Novel functions of the phospholipase D2-phox homology domain in protein kinase C zeta activation

Author(s)
Kim, JHOhba, MSuh, Pann-GhillRyu, SH
Issued Date
2005-04
DOI
10.1128/MCB.25.8.3194-3208.2005
URI
https://scholarworks.unist.ac.kr/handle/201301/10829
Fulltext
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=16244422334
Citation
MOLECULAR AND CELLULAR BIOLOGY, v.25, no.8, pp.3194 - 3208
Abstract
It has been established that protein kinase C zeta (PKC zeta) participates in diverse signaling pathways and cellular functions in a wide variety of cells, exhibiting properties relevant to cellular survival and proliferation. Currently, however, the regulation mechanism of PKC zeta remains elusive. Here, for the first time, we determine that phospholipase D2 (PLD2) enhances PKC zeta activity through direct interaction in a lipase activity-independent manner. This interaction of the PLD2-Phox homology (PX) domain with the PKC zeta-kinase domain also induces the activation loop phosphorylation of PKC zeta and downstream signal stimulation, as measured by p70 S6 kinase phosphorylation. Furthermore, only the PLD2-PX domain directly stimulates PKC zeta activity in vitro, and it is necessary for the formation of the ternary complex with phosphoinositide-dependent kinase I and PKC zeta. The mutant that substitutes the triple lysine residues (Lys(101), Lys(102), and LYS(103)) within the PLD2-PX domain with alanine abolishes interaction with the PKC zeta-kinase domain and activation of PKC zeta. Moreover, breast cancer cell viability is significantly affected by PLD2 silencing. Taken together, these results suggest that the PLD2-mediated PKC zeta activation is induced by its PX domain performing both direct activation of PKC zeta and assistance of activation loop phosphorylation. Furthermore, we find it is an important factor in the survival of breast cancer cells.
Publisher
AMER SOC MICROBIOLOGY
ISSN
0270-7306
Keyword
ADP-RIBOSYLATION FACTORHUMAN BREAST-CANCERFACTOR-REVERSIBLE MANNERP70 S6 KINASEPC12 CELLSINDUCED APOPTOSISDIRECTLY INTERACTSMAMMALIAN-CELLSPLASMA-MEMBRANEBINDING PROTEIN

qrcode

Items in Repository are protected by copyright, with all rights reserved, unless otherwise indicated.