ArticleThe Journal of cell biology2002
Structural requirements for localization and activation of protein kinase C mu (PKC mu) at the Golgi compartment.
Article in The Journal of cell biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 83 citations in OpenAlex.
- PKD3 localizes to late endosomes to maintain Rab7-dependent endolysosomal homeostasis.iScience · 2025Article
- Membrane trafficking in breast cancer progression: protein kinase D comes into play.Frontiers in cell and developmental biology · 2023Review
- The tumor suppressor protein DLC1 maintains protein kinase D activity and Golgi secretory function.The Journal of biological chemistry · 2018Article
- A Rho signaling network links microtubules to PKD controlled carrier transport to focal adhesions.eLife · 2018Article
- Investigation of the Role of Protein Kinase D in Human Rhinovirus Replication.Journal of virology · 2017Article
- A Novel Conserved Domain Mediates Dimerization of Protein Kinase D (PKD) Isoforms: DIMERIZATION IS ESSENTIAL FOR PKD-DEPENDENT REGULATION OF SECRETION AND INNATE IMMUNITY.The Journal of biological chemistry · 2016Article
- Protein Kinase D2 Assembles a Multiprotein Complex at the Trans-Golgi Network to Regulate Matrix Metalloproteinase Secretion.The Journal of biological chemistry · 2016Article
- Protein kinase D promotes plasticity-induced F-actin stabilization in dendritic spines and regulates memory formation.The Journal of cell biology · 2015Article
- A computational model of PKD and CERT interactions at the trans-Golgi network of mammalian cells.BMC systems biology · 2015Article
- The protein kinase D1 COOH terminus: marker or regulator of enzyme activity?American journal of physiology. Cell physiology · 2014Article
- Protein kinase D: a new player among the signaling proteins that regulate functions in the nervous system.Neuroscience bulletin · 2014Review
- Protein kinase D2 induces invasion of pancreatic cancer cells by regulating matrix metalloproteinases.Molecular biology of the cell · 2014Article
- PKD controls mitotic Golgi complex fragmentation through a Raf-MEK1 pathway.Molecular biology of the cell · 2013Article
- Protein kinase D1 mediates anchorage-dependent and -independent growth of tumor cells via the zinc finger transcription factor Snail1.The Journal of biological chemistry · 2012Article
- Regulatory domain determinants that control PKD1 activity.The Journal of biological chemistry · 2012Article
- Global detection of protein kinase D-dependent phosphorylation events in nocodazole-treated human cells.Molecular & cellular proteomics : MCP · 2012Article
- Protein kinase D controls voluntary-running-induced skeletal muscle remodelling.The Biochemical journal · 2011Article
- Phosphorylation of Ser 402 impedes phosphatase activity of slingshot 1.EMBO reports · 2011Article
- A novel protein kinase D phosphorylation site in the tumor suppressor Rab interactor 1 is critical for coordination of cell migration.Molecular biology of the cell · 2011Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We here describe the structural requirements for Golgi localization and a sequential, localization-dependent activation process of protein kinase C (PKC) mu involving auto- and transphosphorylation. The structural basis for Golgi compartment localization was analyzed by confocal microscopy of HeLa cells expressing various PKC mu-green fluorescent protein fusion proteins costained with the Golgi compartment-specific markers p24 and p230. Deletions of either the NH(2)-terminal hydrophobic or the cysteine region, but not of the pleckstrin homology or the acidic domain, of PKC mu completely abrogated Golgi localization of PKC mu. As an NH(2)-terminal PKC mu fragment was colocalized with p24, this region of PKC mu is essential and sufficient to mediate association with Golgi membranes. Fluorescence recovery after photobleaching studies confirmed the constitutive, rapid recruitment of cytosolic PKC mu to, and stable association with, the Golgi compartment independent of activation loop phosphorylation. Kinase activity is not required for Golgi complex targeting, as evident from microscopical and cell fractionation studies with kinase-dead PKC mu found to be exclusively located at intracellular membranes. We propose a sequential activation process of PKC mu, in which Golgi compartment recruitment precedes and is essential for activation loop phosphorylation (serines 738/742) by a transacting kinase, followed by auto- and transphosphorylation of NH(2)-terminal serine(s) in the regulatory domain. PKC mu activation loop phosphorylation is indispensable for substrate phosphorylation and thus PKC mu function at the Golgi compartment.
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