PMID: 9488438Mar 6, 1998

Overexpression of the nucleoporin CAN/NUP214 induces growth arrest, nucleocytoplasmic transport defects, and apoptosis

Molecular and Cellular Biology
J BoerGerard C Grosveld


The human CAN gene was first identified as a target of t(6;9)(p23;q34), associated with acute myeloid leukemia and myelodysplastic syndrome, which results in the expression of a DEK-CAN fusion gene. CAN, also called NUP214, is a nuclear pore complex (NPC) protein that contains multiple FG-peptide sequence motifs. It interacts at the NPC with at least two other proteins, the nucleoporin NUP88 and hCRM1 (exportin 1), which was recently shown to function as a nuclear export receptor. Depletion of CAN in knockout mouse embryonic cells results in cell cycle arrest in G2, followed by inhibition of nuclear protein import and a block of mRNA export. We overexpressed CAN and DEK-CAN in U937 myeloid precursor cells. DEK-CAN expression did not interfere with terminal myeloid differentiation of U937 cells, whereas CAN-overexpressing cells arrested in G0, accumulated mRNA in their nuclei, and died in an apoptotic manner. Interestingly, we found that hCRM1 and import factor p97/importin beta colocalized with the ectopically expressed CAN protein, resulting in depletion of both factors from the NPC. Overexpression of the C-terminal FG-repeat region of CAN, which contains the binding site for hCRM1, caused sequestering of hCRM1 in the nucleopl...Continue Reading


May 15, 1976·International Journal of Cancer. Journal International Du Cancer·C Sundström, K Nilsson
Jun 15, 1992·Proceedings of the National Academy of Sciences of the United States of America·M Gossen, H Bujard
Nov 1, 1992·The Journal of Cell Biology·Y GavrieliS A Ben-Sasson
Jan 1, 1986·Annual Review of Immunology·K Kelly, U Siebenlist
Nov 1, 1994·Journal of Structural Biology·N Panté, U Aebi
Apr 21, 1995·Cell·E Izaurralde, I W Mattaj
Jan 1, 1995·Annual Review of Biochemistry·L I Davis
Jul 3, 1995·Proceedings of the National Academy of Sciences of the United States of America·P ShockettD G Schatz
Jul 1, 1995·The Journal of Cell Biology·N C ChiS A Adam
Jun 1, 1995·Trends in Genetics : TIG·V Doye, E C Hurt
May 9, 1995·Proceedings of the National Academy of Sciences of the United States of America·M González-GarcíaG Nuñez
Feb 28, 1995·Proceedings of the National Academy of Sciences of the United States of America·A RaduM S Moore
Mar 14, 1995·Proceedings of the National Academy of Sciences of the United States of America·J MoroianuA Radu
Jun 1, 1994·Current Opinion in Cell Biology·E Fabre, E C Hurt
Feb 15, 1994·Proceedings of the National Academy of Sciences of the United States of America·D KraemerA Radu
Apr 1, 1994·The Journal of Cell Biology·R W WozniakM P Rout
Mar 15, 1996·Science·D Görlich, I W Mattaj
May 1, 1996·The Journal of Experimental Medicine·D A VignaliJ L Strominger
May 31, 1996·The Journal of Biological Chemistry·C Borner
Dec 6, 1996·Science·C J Sherr
Mar 4, 1997·Proceedings of the National Academy of Sciences of the United States of America·G K FuD M Markovitz
Oct 10, 1997·Cell·Maarten FornerodI W Mattaj


Aug 24, 1999·Brazilian Journal of Medical and Biological Research = Revista Brasileira De Pesquisas Médicas E Biológicas·R Linden, L B Chiarini
Mar 20, 2004·Journal of Neurochemistry·Karine RobertNathalie Janel
Apr 9, 2010·Molecular Biology of the Cell·Masahiro OkaYoshihiro Yoneda
Dec 25, 2012·The Journal of Biological Chemistry·Stephanie RoloffRalph H Kehlenbach
May 26, 1999·Proceedings of the National Academy of Sciences of the United States of America·C ElfgangD Bevec
Nov 15, 2002·International Journal of Hematology·Hisamaru Hirai
Sep 22, 2005·Acta Pharmacologica Sinica·Hong-li LiuJian-feng Zhou
May 29, 2007·Nature Structural & Molecular Biology·Matthew J Gamble, Robert P Fisher
Oct 6, 2009·The Journal of Biological Chemistry·Bo LiuKangling Zhang
Apr 30, 2013·PloS One·Ayten KandilciGerard C Grosveld
Mar 15, 2015·Leukemia·C Sandén, U Gullberg
Jan 24, 2019·Cells·Adélia Mendes, Birthe Fahrenkrog
Jan 4, 2008·Molecular and Cellular Biology·Karen K ResendesDouglass J Forbes
Aug 12, 2006·Canadian Journal of Physiology and Pharmacology·Birthe Fahrenkrog
Feb 21, 2009·Journal of Cellular Biochemistry·Yoshiteru MiyauchiToshimi Michigami
Sep 12, 2018·European Journal of Haematology·Sabine Kayser, Mark J Levis
Jul 21, 2001·Molecular and Cellular Biology·S A BurelD E Zhang
Oct 20, 2006·Proceedings of the National Academy of Sciences of the United States of America·Shu XiaoJian-Hua Tong
Nov 15, 2011·Apoptosis : an International Journal on Programmed Cell Death·Tracey S Hanks, Katherine A Gauss
Jul 28, 2020·Parasitology·Cristian Camilo Galindo, Carlos Arturo Clavijo-Ramírez
May 6, 2006·The Journal of Biological Chemistry·Rafael BernadMaarten Fornerod
Mar 5, 2004·International Journal of Cancer. Journal International Du Cancer·David AgudoJosé Schneider
Jul 29, 2011·Wiley Interdisciplinary Reviews. RNA·Nadeem Siddiqui, Katherine L B Borden
Feb 10, 2021·Modern Pathology : an Official Journal of the United States and Canadian Academy of Pathology, Inc·Hong FangShimin Hu

Related Concepts

NUP214 protein, human
DEK-CAN fusion protein, recombinant
Nup214 protein, mouse
Bcl-XS protein, human
Bcl2l1 protein, mouse
Cell Differentiation Process
Cell Division Phases
Cell Nucleus
Growth Inhibitors

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