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PKC activation by melatonin modulates vimentin intermediate filament organization in N1E‐115 cells
Author(s) -
BenítezKing Gloria
Publication year - 2000
Publication title -
journal of pineal research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.881
H-Index - 131
eISSN - 1600-079X
pISSN - 0742-3098
DOI - 10.1034/j.1600-079x.2000.290102.x
Subject(s) - vimentin , microbiology and biotechnology , protein kinase c , melatonin , intermediate filament , protein kinase a , pinealocyte , biology , phosphorylation , cytoskeleton , map2k7 , chemistry , biochemistry , pineal gland , cyclin dependent kinase 2 , endocrinology , cell , immunohistochemistry , immunology
Melatonin enters cells and causes cytoskeletal rearrangements in unicellular organisms, plants and vertebrates. This pineal secretory product causes microtubule enlargement and neurite outgrowth by a calmodulin antagonism in N1E‐115 cells. Recently, direct in vitro activation of protein kinase C by melatonin was described . Vimentin intermediate filaments are attached to microtubules and their organization depends on both microtubule distribution and phosphorylation of specific proteins. Protein kinase C is a serine threonine kinase which phosphorylates vimentin and through this mechanism causes intermediate filament disassembly. In this work the effects of melatonin on protein kinase C activation, content, and subcellular distribution were studied in N1E‐115 cells. Also, melatonin effects on vimentin phosphorylation and subcellular distribution were explored. The results show that melatonin both activates and increases protein kinase C content in the membrane–cytoskeletal fraction. Melatonin protein kinase C activation was followed by an increase in both vimentin phosphorylation and by vimentin subcellular redistribution. Moreover, staurosporine, a serine threonine kinase inhibitor, prevented increased vimentin phosphorylation elicited by melatonin. Similar effects to those caused by melatonin were obtained with the protein kinase C activator phorbol 12‐myristate 13‐acetate. Data support the idea that melatonin modulates vimentin organization through protein kinase C activation.