2026-04-27T01:59:21Zhttps://repisalud.isciii.es/rest/oai/requestoai:repisalud.isciii.es:20.500.12105/55292024-09-27T08:01:49Zcom_20.500.12105_19604com_20.500.12105_2051col_20.500.12105_19605
Repisalud
author
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
funder
Ministerio de Economía y Competitividad (España)
funder
Unión Europea. Fondo Europeo de Desarrollo Regional (FEDER/ERDF)
funder
Instituto de Salud Carlos III
funder
Progeria Research Foundation
funder
Unión Europea. Comisión Europea
funder
Fundación ProCNIC
2017-12-01T07:37:28Z
2017-12-01T07:37:28Z
2014
PLoS One. 2014; 9(12):e115571
1932-6203
http://hdl.handle.net/20.500.12105/5529
25535984
10.1371/journal.pone.0115571
PLoS ONE
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.
eng
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
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