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oai:repisalud.isciii.es:20.500.12105/55292024-09-27T08:01:49Zcom_20.500.12105_19604com_20.500.12105_2051col_20.500.12105_19605

00925njm 22002777a 4500 dc Gonzalez-Granado, Jose Maria author Navarro-Puche, Ana author Molina-Sanchez, Pedro author Blanco-Berrocal, Marta author Viana, Rosa author Font de Mora, Jaime author Andres, Vicente author 2014 Nuclear 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. PLoS One. 2014; 9(12):e115571 1932-6203 http://hdl.handle.net/20.500.12105/5529 25535984 10.1371/journal.pone.0115571 PLoS ONE A-TYPE LAMINS ENDOPLASMIC-RETICULUM MEMBRANE-PROTEINS CHROMATIN ORGANIZATION MULTIPLE MECHANISMS MUSCULAR-DYSTROPHY C-FOS CELLS TRANSPORT RETROMER Sorting Nexin 6 Enhances Lamin A Synthesis and Incorporation into the Nuclear Envelope