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Myosin VI is associated with secretory granules and is present in the nucleus in adrenal medulla chromaffin cells.
Author(s) -
Łukasz Majewski,
Magdalena Sobczak,
Maria Jolanta Rędowicz
Publication year - 2010
Publication title -
acta biochimica polonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.452
H-Index - 78
eISSN - 1734-154X
pISSN - 0001-527X
DOI - 10.18388/abp.2010_2381
Subject(s) - adrenal medulla , golgi apparatus , nucleus , endoplasmic reticulum , cytoplasm , granule (geology) , medulla , microbiology and biotechnology , secretory vesicle , myosin , gene isoform , actin , chemistry , biology , secretion , exocytosis , biochemistry , endocrinology , gene , catecholamine , paleontology
Myosin VI (MVI) is the only known myosin walking towards minus end of actin filaments. Here, MVI, but not myosins IB or IIB, was detected in chromaffin granules isolated from bovine medulla and found to be tightly associated with the granule apical surface. MVI also localized to secretory granules within rat pheochromocytoma PC12 cells as well as to the Golgi apparatus, endoplasmic reticulum and clathrin-coated pits. Notably, it was also found in the nucleus. RT-PCR revealed that MVI splice variants with a large insert (LI), characteristic of polarized cells, were barely detectable in PC12 cells, whereas variants with a small insert (SI) were the major isoforms. The presented data indicate that MVI in adrenal medulla cells is engaged in secretory vesicle trafficking within the cytoplasm and possibly also involved in transport within the nucleus.

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