ArticleProceedings of the National Academy of Sciences of the United States of America1994
Phospholipase C-gamma 1 binding to intracellular receptors for activated protein kinase C.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Protein Kinase C Regulates Meiosis in Mammalian Oocytes.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- Molecular Cloning, Characterization, and Expression of a Receptor for Activated Protein Kinase C1 (RACK1) Gene inBiology · 2024Article
- Recent Advances in Monoclonal Antibody Therapy for Colorectal Cancers.Biomedicines · 2021Review
- The RNA-binding protein SERBP1 interacts selectively with the signaling protein RACK1.Cellular signalling · 2017Article
- RACK1 regulates angiotensin II-induced contractions of SHR preglomerular vascular smooth muscle cells.American journal of physiology. Renal physiology · 2017Article
- 'Medusa head ataxia': the expanding spectrum of Purkinje cell antibodies in autoimmune cerebellar ataxia. Part 2: Anti-PKC-gamma, anti-GluR-delta2, anti-Ca/ARHGAP26 and anti-VGCC.Journal of neuroinflammation · 2015Review
- Review
- AXL mediates resistance to PI3Kα inhibition by activating the EGFR/PKC/mTOR axis in head and neck and esophageal squamous cell carcinomas.Cancer cell · 2015Article
- Protein kinase C (PKC) activity regulates functional effects of Kvβ1.3 subunit on KV1.5 channels: identification of a cardiac Kv1.5 channelosome.The Journal of biological chemistry · 2012Article
- Signaling of the direction-sensing FAK/RACK1/PDE4D5 complex to the small GTPase Rap1.Small GTPases · 2011Article
- Identification of phospholipase C gamma1 as a protein tyrosine phosphatase mu substrate that regulates cell migration.Journal of cellular biochemistry · 2011Article
- Rationally designed peptide regulators of protein kinase C.Trends in endocrinology and metabolism: TEM · 2009Review
- Modulation of NMDA receptors by pituitary adenylate cyclase activating peptide in CA1 neurons requires G alpha q, protein kinase C, and activation of Src.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2005Article
- Muscle ring finger protein-1 inhibits PKC{epsilon} activation and prevents cardiomyocyte hypertrophy.The Journal of cell biology · 2004Article
- Interaction of "readthrough" acetylcholinesterase with RACK1 and PKCbeta II correlates with intensified fear-induced conflict behavior.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Review
- Cloning of a WD-repeat-containing gene from alfalfa (Medicago sativa): a role in hormone-mediated cell division?Plant molecular biology · 1997Article
- Article
- The cpc-2 gene of Neurospora crassa encodes a protein entirely composed of WD-repeat segments that is involved in general amino acid control and female fertility.Molecular & general genetics : MGG · 1995Article
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Authors and funding
5 authors.
Funding
Abstract
Phospholipase C-gamma 1 (PLC-gamma 1; EC 3.1.4.11) hydrolyzes phosphatidylinositol 4,5-bisphosphate to generate diacylglycerol and inositol 1,4,5-trisphosphate and is activated in response to growth factor stimulation and tyrosine phosphorylation. Concomitantly, the enzyme translocates from the cytosol to the particulate cell fraction. A similar process of activation-induced translocation from the cytosol to the cell particulate fraction has also been described for protein kinase C (PKC). We have previously shown that activated PKC binds to specific receptor proteins, receptors for activated C kinase, or RACKs, of approximately 30 kDa. Here, we show that PLC-gamma 1 bound to these RACKs and inhibited subsequent PKC binding to RACKs. However, unlike PKC, the binding of PLC-gamma 1 to RACKs did not require phospholipids and calcium. After epidermal growth factor treatment of intact A-431 cells, the binding of PLC-gamma 1 to RACKs increased as compared with PLC-gamma 1 from control cells. This increase in PLC-gamma 1 binding to RACKs was due to the phosphorylation of PLC-gamma 1. Additional data indicated that PLC-gamma 1 binds to RACKs in solution; epidermal growth factor receptor-dependent PLC-gamma 1 phosphorylation and activation decreased in the presence of RACKs. It is possible that, in vivo, PLC-gamma 1 associates with RACKs or with other PLC-gamma 1-specific anchoring proteins in the particulate cell fraction. Since a PKC C2 homologous region is present in PLC-gamma 1, the C2 region may mediate the activation-induced translocation of the enzyme to the cell particulate fraction and the anchoring protein-PLC-gamma 1 complex may be the active translocated form of PLC-gamma 1.
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