Structural characterization and subcellular localization of Drosophila organic solute carrier partner 1
| Autor: | Takanari Umegawachi, Masamitsu Yamaguchi, Hideki Yoshida, Nguyen Tho Huu, Seiji Miyata |
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| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Biochemistry
Cell membrane symbols.namesake medicine Animals Drosophila Proteins Humans Organic solute carrier partner 1 Molecular Biology Phylogeny biology Molecular Structure Membrane transport protein Endoplasmic reticulum Cell Membrane Membrane Transport Proteins Golgi apparatus Subcellular localization Recombinant Proteins Transport protein Solute carrier family Cell biology Protein Transport medicine.anatomical_structure Larva biology.protein symbols Drosophila Subcellular organelle Transcriptome Dimerization Sequence Alignment Drosophila Protein Research Article |
| Zdroj: | BMC Biochemistry |
| ISSN: | 1471-2091 |
| Popis: | Background Organic solute carrier partner 1 (OSCP1) is known to facilitate the transport of various organic solutes into cells and reported to play a role in cell growth and cell differentiation. Moreover, OSCP1 is known as a tumor suppressor gene that is frequently down-expressed in nasopharyngeal carcinomas and acute myeloid leukemia. However, the underlying mechanisms of action remain unclear and the subcellular localization of OSCP1 has yet to be determined in detail. Results Drosophila contains a single orthologue of OSCP1 (dOSCP1) that shares 58% homology with its human counterpart. To study the expression pattern and subcellular localization of dOSCP1, we prepared a specific antibody. Subcellular localization analyses of dOSCP1 with these revealed localization in the plasma membrane, endoplasmic reticulum, Golgi apparatus and mitochondria, but no detection in cytosol. dOSCP1 signals were also detected in the nucleus, although at weaker intensity than in plasma membranes and subcellular organelles. In addition, native polyacrylamide gel electrophoresis analysis with and without β-mercaptoethanol treatment revealed that recombinant dOSCP1 forms dimers and trimers in solution. The dimer form of dOSCP1 could also be detected by Western immunoblot analyses in third instar larval extracts. Conclusions The data revealed that dOSCP1 localizes not only in the plasma membrane but also in the nucleus, ER, Golgi apparatus and mitochondria. It is therefore conceivable that this protein may interact with various partners or form multimeric complexes with other proteins to play multiple roles in cells, providing clues to understanding the functions of dOSCP1 during Drosophila development. |
| Databáze: | OpenAIRE |
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