Journal article
ARF1-regulated coatomer directs the steady-state localization of protein kinase C epsilon at the Golgi apparatus
Biochimica et biophysica acta. Molecular cell research, Vol.1833(3), pp.487-493
03/01/2013
DOI: 10.1016/j.bbamcr.2012.11.011
PMCID: PMC4831130
PMID: 23195223
Abstract
Protein kinase C epsilon (PKC epsilon) contributes to multiple signaling pathways affecting human disease. The function of PKC epsilon requires it to undergo changes in subcellular distribution in response to signaling events. While the mechanisms underlying this translocation are incompletely understood, it involves the receptor for activated C kinase protein (RACK2/beta'-COP). This receptor also functions as a vesicle coat protein in the secretory pathway where it is regulated by the small GTP-binding protein ADP-ribosylation factor, ARF1. We inhibited ARF1 activation to test the requirement for RACK2/beta'-COP in PKC epsilon localization in NIH3T3 fibroblasts. We found that steady-state localization of PKC epsilon at the Golgi complex requires ARF1-regulated RACK2/beta'-COP function. By contrast, we did not observe any defects in phorbol ester-induced translocation when ARF1 was inhibited. We also found that PKC epsilon bound to isolated membranes through two distinct mechanisms. One mechanism was dependent upon RACK2/beta'-COP while a second was RACK2/beta'-COP-independent and stimulated by phorbol esters. Finally, we show that RACK2/beta'-COP affects the subcellular distribution of a constitutively active form of PKC epsilon, in a manner similar to what we observed for wild-type PKC epsilon. Together, our data support a role for RACK2/beta'-COP in the steady-state localization of PKC epsilon at the Golgi apparatus, which may be independent of its role during PKC epsilon translocation to the cell surface. (C) 2012 Elsevier B.V. All rights reserved.
Details
- Title: Subtitle
- ARF1-regulated coatomer directs the steady-state localization of protein kinase C epsilon at the Golgi apparatus
- Creators
- Tabitha A. Peterson - Roy J. and Lucille A. Carver College of MedicineMark Stamnes - Roy J. and Lucille A. Carver College of Medicine
- Resource Type
- Journal article
- Publication Details
- Biochimica et biophysica acta. Molecular cell research, Vol.1833(3), pp.487-493
- DOI
- 10.1016/j.bbamcr.2012.11.011
- PMID
- 23195223
- PMCID
- PMC4831130
- NLM abbreviation
- Biochim Biophys Acta Mol Cell Res
- ISSN
- 0167-4889
- eISSN
- 1879-2596
- Publisher
- Elsevier
- Number of pages
- 7
- Grant note
- HL07344-32 / Program in Hematology: Molecular and Cell Biology of Blood Cells at the University of Iowa, NIH T32HL007344 / NATIONAL HEART, LUNG, AND BLOOD INSTITUTE; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA; NIH National Heart Lung & Blood Institute (NHLBI) Carver Medical Research Initiative Grant, Carver College of Medicine, University of Iowa
- Language
- English
- Date published
- 03/01/2013
- Academic Unit
- Molecular Physiology and Biophysics; Internal Medicine
- Record Identifier
- 9984297604202771
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