Structure and Function of the Nuclear Pore Complex

1992 ◽  
Vol 8 (1) ◽  
pp. 495-527 ◽  
Author(s):  
D J Forbes
1995 ◽  
pp. 89-92 ◽  
Author(s):  
N. Pante ◽  
R. Bastos ◽  
I. McMorrow ◽  
K. N. Goldie ◽  
B. Burke ◽  
...  

2008 ◽  
Vol 129 (2) ◽  
pp. 105-116 ◽  
Author(s):  
Roderick Y. H. Lim ◽  
Ueli Aebi ◽  
Birthe Fahrenkrog

2002 ◽  
Vol 158 (5) ◽  
pp. 915-927 ◽  
Author(s):  
Janet M. Cronshaw ◽  
Andrew N. Krutchinsky ◽  
Wenzhu Zhang ◽  
Brian T. Chait ◽  
Michael J. Matunis

As the sole site of nucleocytoplasmic transport, the nuclear pore complex (NPC) has a vital cellular role. Nonetheless, much remains to be learned about many fundamental aspects of NPC function. To further understand the structure and function of the mammalian NPC, we have completed a proteomic analysis to identify and classify all of its protein components. We used mass spectrometry to identify all proteins present in a biochemically purified NPC fraction. Based on previous characterization, sequence homology, and subcellular localization, 29 of these proteins were classified as nucleoporins, and a further 18 were classified as NPC-associated proteins. Among the 29 nucleoporins were six previously undiscovered nucleoporins and a novel family of WD repeat nucleoporins. One of these WD repeat nucleoporins is ALADIN, the gene mutated in triple-A (or Allgrove) syndrome. Our analysis defines the proteome of the mammalian NPC for the first time and paves the way for a more detailed characterization of NPC structure and function.


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