What question did this study set out to answer?

To determine the mutual protein interactions and precise three-dimensional localization of O-linked glycoprotein components within the nuclear pore complex.

August 1, 1994The Journal of Cell BiologyOpen Access

Interactions and three-dimensional localization of a group of nuclear pore complex proteins.

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Authors

NPNelly PantéUniversity of British Columbia RBRicardo BastosHospital Pedro Hispano IMIsabel M. McMorrowMassachusetts General Hospital

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Implication

Structural analysis reveals specific subcomplexes and 3D positioning of p250, NUP153, and p62 in the nuclear pore complex, highlighting structural organization across the nuclear envelope.

Key Points

To determine the mutual protein interactions and precise three-dimensional localization of O-linked glycoprotein components within the nuclear pore complex.
Western blotting and immunofluorescence microscopy of cultured cell lines using monoclonal antibody QE5, which recognizes p250, NUP153, and p62.
Biochemical extraction via detergent and high-salt treatment to analyze protein complexes, alongside in vitro galactosylation assays.
High-resolution electron microscopy of Xenopus oocyte nuclear envelopes using quick freezing, freeze drying, rotary metal shadowing, and gold-conjugated antibody or wheat germ agglutinin labeling.
Detergent and high-salt extraction released p250 complexed with a novel 75 kD protein, NUP153 as a ~1 MDa homo-oligomer, and p62 associated with 58 kD and 54 kD polypeptides.
Immunogold electron microscopy mapped QE5 epitopes to both the cytoplasmic filaments and the nuclear basket of the nuclear pore complex.
Specific antibody labeling demonstrated that p250 localizes to the cytoplasmic filaments, whereas NUP153 resides in the nuclear basket with an epitope at the terminal ring.

Cite This Study

Panté et al. (1994) studied this question.

synapsesocial.com/papers/6a9029eb1dcd98381b83ff0c https://doi.org/10.1083/jcb.126.3.603

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Implication

Structural analysis reveals specific subcomplexes and 3D positioning of p250, NUP153, and p62 in the nuclear pore complex, highlighting structural organization across the nuclear envelope.

Interactions and three-dimensional localization of a group of nuclear pore complex proteins.

Discussion

Member takes

Implication

Key Points

Cite This Study

Interactions and three-dimensional localization of a group of nuclear pore complex proteins.

Discussion

Member takes

Implication

Key Points

Cite This Study

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