BREK/LMTK2 is a myosin VI-binding protein involved in endosomal membrane trafficking

التفاصيل البيبلوغرافية
العنوان: BREK/LMTK2 is a myosin VI-binding protein involved in endosomal membrane trafficking
المؤلفون: Takahide Kon, Reiko Ohkura, Takeshi Inoue, Kazuo Sutoh, Hisashi Yamakawa, Jun Yokota, Osamu Ohara
المصدر: Genes to Cells. 13:483-495
بيانات النشر: Wiley, 2008.
سنة النشر: 2008
مصطلحات موضوعية: Cytoplasm, Endosome, Endocytic cycle, Down-Regulation, Endosomes, Protein Serine-Threonine Kinases, Biology, Endocytosis, LMTK2, Cell Line, symbols.namesake, Two-Hybrid System Techniques, Myosin, Genetics, Animals, Humans, RNA, Small Interfering, Transport Vesicles, Myosin Heavy Chains, Vesicle, Transferrin, Membrane Proteins, Cell Biology, Golgi apparatus, Transmembrane protein, Cell biology, symbols
الوصف: Myosin VI is involved in a wide range of endocytic and exocytic membrane trafficking pathways; clathrin-mediated endocytosis, intracellular transport of clathrin-coated and -uncoated vesicles, AP-1B-dependent basolateral sorting in polarized epithelial cells and secretion from the Golgi complex to the cell surface. In this study, using a yeast two-hybrid screen, we identified brain-enriched kinase/lemur tyrosine kinase 2 (BREK/LMTK2), a transmembrane serine/threonine kinase with previously unknown cellular functions, as a myosin VI-interacting protein. Several binding experiments confirmed the interaction of myosin VI with BREK in vivo and in vitro. Immunocytochemical analyses revealed that BREK localizes to cytoplasmic membrane vesicles and to perinuclear recycling endosomes. Notably, cells in which BREK was depleted by siRNA were still able to internalize transferrin molecules and to transport them to early endosomes, but were unable to transport them to perinuclear recycling endosomes. Our results show that BREK is critical for the transition of endocytosed membrane vesicles from early endosomes to recycling endosomes and also suggest an involvement of myosin VI in this pathway.
تدمد: 1365-2443
1356-9597
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a5a757e1f9f362cc64c01cf5fd885eeTest
https://doi.org/10.1111/j.1365-2443.2008.01184.xTest
حقوق: CLOSED
رقم الانضمام: edsair.doi.dedup.....8a5a757e1f9f362cc64c01cf5fd885ee
قاعدة البيانات: OpenAIRE