ArticleMolecular and cellular biology2005
Novel functions of the phospholipase D2-Phox homology domain in protein kinase Czeta activation.
Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 38 citations in OpenAlex.
- Phospholipase D2 is a positive regulator of sirtuin 1 and modulates p53-mediated apoptosis via sirtuin 1.Experimental & molecular medicine · 2021Article
- The phospholipase D inhibitor FIPI potently blocks EGF-induced calcium signaling in human breast cancer cells.Cell communication and signaling : CCS · 2021Article
- Mammalian phospholipase D: Function, and therapeutics.Progress in lipid research · 2020Review
- Phospholipase D1 Signaling: Essential Roles in Neural Stem Cell Differentiation.Journal of molecular neuroscience : MN · 2018Review
- Hippocalcin Promotes Neuronal Differentiation and Inhibits Astrocytic Differentiation in Neural Stem Cells.Stem cell reports · 2017Article
- Modulation of PKC signaling and induction of apoptosis through suppression of reactive oxygen species and tumor necrosis factor receptor 1 (TNFR1): key role of quercetin in cancer prevention.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2015Article
- Mechanism of enzymatic reaction and protein-protein interactions of PLD from a 3D structural model.Cellular signalling · 2015Article
- Phosphatidic acid, phospholipase D and tumorigenesis.Advances in biological regulation · 2014Article
- Phospholipase D2 mediates signaling by ATPase class I type 8B membrane 1.Journal of lipid research · 2013Article
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- Nonmuscle myosin II is required for internalization of the epidermal growth factor receptor and modulation of downstream signaling.The Journal of biological chemistry · 2012Article
- Differential dephosphorylation of the protein kinase C-zeta (PKCζ) in an integrin αIIbβ3-dependent manner in platelets.Biochemical pharmacology · 2011Article
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- Targeting phospholipase D with small-molecule inhibitors as a potential therapeutic approach for cancer metastasis.Future oncology (London, England) · 2009Review
- House dust mite allergen Der f 2-induced phospholipase D1 activation is critical for the production of interleukin-13 through activating transcription factor-2 activation in human bronchial epithelial cells.The Journal of biological chemistry · 2009Article
- Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It has been established that protein kinase Czeta (PKCzeta) 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 PKCzeta remains elusive. Here, for the first time, we determine that phospholipase D2 (PLD2) enhances PKCzeta activity through direct interaction in a lipase activity-independent manner. This interaction of the PLD2-Phox homology (PX) domain with the PKCzeta-kinase domain also induces the activation loop phosphorylation of PKCzeta and downstream signal stimulation, as measured by p70 S6 kinase phosphorylation. Furthermore, only the PLD2-PX domain directly stimulates PKCzeta activity in vitro, and it is necessary for the formation of the ternary complex with phosphoinositide-dependent kinase 1 and PKCzeta. The mutant that substitutes the triple lysine residues (Lys101, Lys102, and Lys103) within the PLD2-PX domain with alanine abolishes interaction with the PKCzeta-kinase domain and activation of PKCzeta. Moreover, breast cancer cell viability is significantly affected by PLD2 silencing. Taken together, these results suggest that the PLD2-mediated PKCzeta activation is induced by its PX domain performing both direct activation of PKCzeta and assistance of activation loop phosphorylation. Furthermore, we find it is an important factor in the survival of breast cancer cells.
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