ArticleMolecular biology of the cell1997
14-3-3 inhibits the Dictyostelium myosin II heavy-chain-specific protein kinase C activity by a direct interaction: identification of the 14-3-3 binding domain.
Article in Molecular biology of the cell, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 28 citations in OpenAlex.
- Targeting lysine-specific demethylase 1A inhibits renal epithelial-mesenchymal transition and attenuates renal fibrosis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022Article
- Comparative Proteomics of Purified Pathogen Vacuoles Correlates Intracellular Replication ofMolecular & cellular proteomics : MCP · 2017Article
- The yeast 14-3-3 proteins BMH1 and BMH2 differentially regulate rapamycin-mediated transcription.Bioscience reports · 2014Article
- A 20-amino acid module of protein kinase C{epsilon} involved in translocation and selective targeting at cell-cell contacts.The Journal of biological chemistry · 2009Article
- 14-3-3 proteins interact with the beta-thymosin repeat protein Csp24.Neuroscience letters · 2007Article
- Expression of 14-3-3 zeta and interaction with protein kinase C in the rat retina in early diabetes.Diabetologia · 2005Article
- Protein kinase Cepsilon actin-binding site is important for neurite outgrowth during neuronal differentiation.Molecular biology of the cell · 2002Article
- Localization of fission yeast type II myosin, Myo2, to the cytokinetic actin ring is regulated by phosphorylation of a C-terminal coiled-coil domain and requires a functional septation initiation network.Molecular biology of the cell · 2001Article
- Protein kinase C activation by acidic proteins including 14-3-3.The Biochemical journal · 2000Article
- Specific interactions with TBP and TFIIB in vitro suggest that 14-3-3 proteins may participate in the regulation of transcription when part of a DNA binding complex.The Plant cell · 1999Article
- alpha-Synuclein shares physical and functional homology with 14-3-3 proteins.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1999Article
- PKCepsilon, via its regulatory domain and independently of its catalytic domain, induces neurite-like processes in neuroblastoma cells.The Journal of cell biology · 1999Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Myosin II heavy chain (MHC) specific protein kinase C (MHC-PKC), isolated from Dictyostelium discoideum, regulates myosin II assembly and localization in response to the chemoattractant cyclic AMP. Immunoprecipitation of MHC-PKC revealed that it resides as a complex with several proteins. We show herein that one of these proteins is a homologue of the 14-3-3 protein (Dd14-3-3). This protein has recently been implicated in the regulation of intracellular signaling pathways via its interaction with several signaling proteins, such as PKC and Raf-1 kinase. We demonstrate that the mammalian 14-3-3 zeta isoform inhibits the MHC-PKC activity in vitro and that this inhibition is carried out by a direct interaction between the two proteins. Furthermore, we found that the cytosolic MHC-PKC, which is inactive, formed a complex with Dd14-3-3 in the cytosol in a cyclic AMP-dependent manner, whereas the membrane-bound active MHC-PKC was not found in a complex with Dd14-3-3. This suggests that Dd14-3-3 inhibits the MHC-PKC in vivo. We further show that MHC-PKC binds Dd14-3-3 as well as 14-3-3 zeta through its C1 domain, and the interaction between these two proteins does not involve a peptide containing phosphoserine as was found for Raf-1 kinase. Our experiments thus show an in vivo function for a member of the 14-3-3 family and demonstrate that MHC-PKC interacts directly with Dd14-3-3 and 14-3-3 zeta through its C1 domain both in vitro and in vivo, resulting in the inhibition of the kinase.
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