BROWSE

Related Researcher

Author's Photo

Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

ITEM VIEW & DOWNLOAD

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

Cited 23 times inthomson ciCited 20 times inthomson ci
Title
Novel functions of the phospholipase D2-phox homology domain in protein kinase C zeta activation
Author
Kim, JHKim, JHOhba, MSuh, Pann-GhillRyu, SH
Keywords
ADP-RIBOSYLATION FACTOR; HUMAN BREAST-CANCER; FACTOR-REVERSIBLE MANNER; P70 S6 KINASE; PC12 CELLS; INDUCED APOPTOSIS; DIRECTLY INTERACTS; MAMMALIAN-CELLS; PLASMA-MEMBRANE; BINDING PROTEIN
Issue Date
2005-04
Publisher
AMER SOC MICROBIOLOGY
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.
URI
Go to Link
DOI
10.1128/MCB.25.8.3194-3208.2005
ISSN
0270-7306
Appears in Collections:
BME_Journal Papers
Files in This Item:
000228138500028.pdf Download

find_unist can give you direct access to the published full text of this article. (UNISTARs only)

Show full item record

qrcode

  • mendeley

    citeulike

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

MENU