title: The Golgi-associated long coiled-coil protein NECC1 participates in the control of the regulated secretory pathway in PC12 cells.
abstract: Golgi-associated long coiled-coil proteins, often referred to as golgins, are involved in the maintenance of the structural organization of the Golgi apparatus and the regulation of membrane traffic events occurring in this organelle. Little information is available on the contribution of golgins to Golgi function in cells specialized in secretion such as endocrine cells or neurons. In the present study, we characterize the intracellular distribution as well as the biochemical and functional properties of a novel long coiled-coil protein present in neuroendocrine tissues, NECC1 (neuroendocrine long coiled-coil protein 1). The present study shows that NECC1 is a peripheral membrane protein displaying high stability to detergent extraction, which distributes across the Golgi apparatus in neuroendocrine cells. In addition, NECC1 partially localizes to post-Golgi carriers containing secretory cargo in PC12 cells. Overexpression of NECC1 resulted in the formation of juxtanuclear aggregates together with a slight fragmentation of the Golgi and a decrease in K+-stimulated hormone release. In contrast, NECC1 silencing did not alter Golgi architecture, but enhanced K+-stimulated hormone secretion in PC12 cells. In all, the results of the present study identify NECC1 as a novel component of the Golgi matrix and support a role for this protein as a negative modulator of the regulated trafficking of secretory cargo in neuroendocrine cells.
authors.affiliation: Department of Cell Biology, Physiology and Immunology, Instituto Maimónides de Investigación Biomédica de Córdoba (IMIBIC), University of Córdoba, Cordoba, Spain.
authors.forename: David
authors.initials: D
authors.lastname: Cruz-García
authors.forename: Alberto
authors.initials: A
authors.lastname: Díaz-Ruiz
authors.forename: Yoana
authors.initials: Y
authors.lastname: Rabanal-Ruiz
authors.forename: Juan R
authors.initials: JR
authors.lastname: Peinado
authors.forename: Francisco
authors.initials: F
authors.lastname: Gracia-Navarro
authors.forename: Justo P
authors.initials: JP
authors.lastname: Castaño
authors.forename: Maité
authors.initials: M
authors.lastname: Montero-Hadjadje
authors.forename: Marie-Christine
authors.initials: MC
authors.lastname: Tonon
authors.forename: Hubert
authors.initials: H
authors.lastname: Vaudry
authors.forename: Youssef
authors.initials: Y
authors.lastname: Anouar
authors.forename: Rafael
authors.initials: R
authors.lastname: Vázquez-Martínez
authors.forename: María M
authors.initials: MM
authors.lastname: Malagón
mesh_terms: D000818:Animals; D001692:Biological Transport; D020868:Gene Silencing; D006056:Golgi Apparatus / Q000378:metabolism*; D018398:Homeodomain Proteins / Q000235:genetics / Q000378:metabolism*; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D055099:Neuroendocrine Cells / Q000378:metabolism; D016716:PC12 Cells; D051381:Rats
chemical_list: D018398:Homeodomain Proteins; C572070:Jakmip2 protein, rat; D008565:Membrane Proteins