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Sorting nexin 6 enhances lamin a synthesis and incorporation into the nuclear envelope

AuthorsGonzález-Granado, José M. ; Navarro-Puche, Ana; Molina-Sanchez, Pedro; Blanco-Berrocal, Marta; Viana, Rosa ; Font de Mora, Jaime; Andrés, Vicente
Issue Date23-Dec-2014
PublisherPublic Library of Science
CitationPLoS ONE 9(12):e115571. (2014)
AbstractNuclear lamins are important structural and functional proteins in mammalian cells, but little is known about the mechanisms and cofactors that regulate their traffic into the nucleus. Here, we demonstrate that trafficking of lamin A, but not lamin B1, and its assembly into the nuclear envelope are regulated by sorting nexin 6 (SNX6), a major component of the retromer that targets proteins and other molecules to specific subcellular locations. SNX6 interacts with lamin A in vitro and in vivo and links it to the outer surface of the endoplasmic reticulum in human and mouse cells. SNX6 transports its lamin A cargo to the nuclear envelope in a process that takes several hours. Lamin A protein levels in the nucleus augment or decrease, respectively, upon gain or loss of SNX6 function. We further show that SNX6-dependent lamin A nuclear import occurs across the nuclear pore complex via a RAN-GTP-dependent mechanism. These results identify SNX6 as a key regulator of lamin A synthesis and incorporation into the nuclear envelope.
Description25 páginas, 6 figuras. Enlaces a 4 figuras y 2 videos desde supporting information
Publisher version (URL)http://dx.doi.org/10.1371/journal.pone.0115571
Appears in Collections:(IBV) Artículos
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