| Subcellular localization analysis of the closely related Fps/Fes and Fer protein-tyrosine kinases suggests a distinct role for Fps/Fes in vesicular trafficking. | |
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MedLine Citation:
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PMID: 11339827 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The subcellular localizations of the Fps/Fes and closely related Fer cytoplasmic tyrosine kinases were studied using green fluorescent protein (GFP) fusions and confocal fluorescence microscopy. In contrast to previous reports, neither kinase localized to the nucleus. Fer was diffusely cytoplasmic throughout the cell cycle. Fps/Fes also displayed a diffuse cytoplasmic localization, but in addition it showed distinct accumulations in cytoplasmic vesicles as well as in a perinuclear region consistent with the Golgi. This localization was very similar to that of TGN38, a known marker of the trans Golgi. The localization of Fps/Fes and TGN38 were both perturbed by brefeldin A, a fungal metabolite that disrupts the Golgi apparatus. Fps/Fes was also found to colocalize to various extents with several Rab proteins, which are members of the monomeric G-protein superfamily involved in vesicular transport between specific subcellular compartments. Using Rabs that are involved in endocytosis (Rab5B and Rab7) or exocytosis (Rab1A and Rab3A), we showed that Fps/Fes is localized in both pathways. These results suggest that Fps/Fes may play a general role in the regulation of vesicular trafficking. |
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Authors:
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R Zirngibl; D Schulze; S E Mirski; S P Cole; P A Greer |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Experimental cell research Volume: 266 ISSN: 0014-4827 ISO Abbreviation: Exp. Cell Res. Publication Date: 2001 May |
Date Detail:
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Created Date: 2001-05-07 Completed Date: 2001-06-14 Revised Date: 2012-06-01 |
Medline Journal Info:
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Nlm Unique ID: 0373226 Medline TA: Exp Cell Res Country: United States |
Other Details:
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Languages: eng Pagination: 87-94 Citation Subset: IM |
Copyright Information:
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Copyright 2001 Academic Press. |
Affiliation:
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Cancer Research Laboratories, Queen's University, Kingston, Ontario K7L 3N6, Canada. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals COS Cells / cytology, metabolism Cell Compartmentation / physiology* Cell Cycle / physiology Cytoplasm / metabolism*, ultrastructure Fusion Proteins, gag-onc / metabolism* Glycoproteins* Golgi Apparatus / metabolism Immunohistochemistry Intracellular Membranes / metabolism Membrane Glycoproteins / metabolism Membrane Proteins* Protein Transport / physiology* Protein-Tyrosine Kinases* Proto-Oncogene Proteins / metabolism* Transport Vesicles / metabolism*, ultrastructure rab GTP-Binding Proteins / metabolism |
| Chemical | |
Reg. No./Substance:
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0/Fusion Proteins, gag-onc; 0/Glycoproteins; 0/Membrane Glycoproteins; 0/Membrane Proteins; 0/Proto-Oncogene Proteins; 110736-90-8/proto-oncogene protein c-fes-fps; EC 2.7.10.1/Protein-Tyrosine Kinases; EC 2.7.10.2/v-fps oncogene protein, Fujinami sarcoma virus; EC 3.6.1.-/rab GTP-Binding Proteins |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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