Proteomic analysis of the mammalian nuclear pore complex.
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.
Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205, USA.
Janet M
JM
Cronshaw
Andrew N
AN
Krutchinsky
Wenzhu
W
Zhang
Brian T
BT
Chait
Michael J
MJ
Matunis
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D019143:Evolution, Molecular; D006367:HeLa Cells; D006801:Humans; D008099:Liver / Q000166:cytology; D013058:Mass Spectrometry; D008854:Microscopy, Electron; D008970:Molecular Weight; D022022:Nuclear Pore / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D028861:Nuclear Pore Complex Proteins / Q000032:analysis / Q000737:chemistry* / Q000145:classification / Q000302:isolation & purification*; D040901:Proteomics; D051381:Rats; D014162:Transfection
D028861:Nuclear Pore Complex Proteins